Patent Description:
Textiles are used to make shirts, pants, dresses, skirts, coats, blouses, t-shirts, sweaters, shoes, bags, furniture, blankets, curtains, wall coverings, table cloths, car seats and interiors, medical/biomedical devices, disposable hygiene products, insulation and landscaping materials, tents, sails, boat, aircraft exteriors and the like. Textiles come with a variety of different properties such as stretchability, breathability, high tear strength, elongation and elasticity, absorbency and wicking, loft and resiliency, drape, strength and abrasion resistance. There is a continuing need for fibers, yarns, threads and textiles with unique aesthetics and properties.

Some embodiments described herein are directed to a method for forming protein-coated materials including coating a substrate selected from the group consisting of a sheet, a textile, a rope, a fiber, a strand, and a yarn with a salt solution, drying the substrate, and coating the substrate with a protein.

Some embodiments described herein are directed to a method for forming protein-coated materials including coating a substrate selected from the group consisting of a sheet, a textile, a rope, a fiber, a strand, and a yarn with a solution of a polymer that is immiscible with the protein, and subsequently coating the substrate with the protein.

All methods and materials similar or equivalent to those described herein can be used in the practice or testing of embodiments described herein, with suitable methods and materials being described herein. The materials, methods, and examples are illustrative only and are not intended to be limiting, unless otherwise specified.

The indefinite articles "a," "an," and "the" include plural referents unless clearly contradicted or the context clearly dictates otherwise.

The term "comprising" is an open-ended transitional phrase. A list of elements following the transitional phrase "comprising" is a non-exclusive list, such that elements in addition to those specifically recited in the list can also be present. The phrase "consisting essentially of" limits the composition of a component to the specified materials and those that do not materially affect the basic and novel characteristic(s) of the component. The phrase "consisting of" limits the composition of a component to the specified materials and excludes any material not specified.

Where a range of numerical values comprising upper and lower values is recited herein, unless otherwise stated in specific circumstances, the range is intended to include the endpoints thereof, and all integers and fractions within the range. It is not intended that the disclosure or claims be limited to the specific values recited when defining a range. Further, when an amount, concentration, or other value or parameter is given as a range, one or more ranges, or as list of upper values and lower values, this is to be understood as specifically disclosing all ranges formed from any pair of any upper range limit or value and any lower range limit or value, regardless of whether such pairs are separately disclosed. Finally, when the term "about" is used in describing a value or an end-point of a range, the disclosure should be understood to include the specific value or end-point referred to. Whether or not a numerical value or end-point of a range recites "about," the numerical value or end-point of a range is intended to include two embodiments: one modified by "about," and one not modified by "about.

As used herein, the term "about" refers to a value that is within ± <NUM>% of the value stated. For example, about <NUM> kPa can include any number between <NUM> kPa and <NUM> kPa.

As used herein, a substrate means a sheet, a textile, a rope, a fiber, a strand, or a yarn.

As used herein, a strand means a single ply yarn; one strand of fiber that is twisted into a yarn. The physical properties and dimensions of the strand can vary depending on the type of fiber. The diameter of a single ply yarn can be <NUM> (millimeters) or more.

As used herein, yarn means ply-yarn where two or more strands are twisted together. The yarn diameter can range from about <NUM> to about <NUM>, about <NUM> to about <NUM>, about <NUM> to about <NUM>, or about <NUM> to about <NUM>.

As used herein, thread means tightly twisted plied yarn used for sewing with a diameter ranging from about <NUM> to about <NUM>, about <NUM> to about <NUM>, or about <NUM> to about <NUM>.

As used herein, a rope is a thick cord; a cord is made by twisting ply yarns together. Some types of sewing thread and ropes are cords. Cord yarns are seldom used in apparel or interior fabrics but are used in technical fabrics such as duck and canvas. Cord yarns can be <NUM> or more in diameter, and can consist of strands of fiber, leather, wire, or other materials that are braided or twisted together. Creating a rope through the process of braiding or twisting is called laying. Ropes are technical items where high performance is expected. Ropes are used in a wide variety of uses including farming and agricultural operations, utility work, commercial and recreational fishing, sailing vessels, shipping, transportation, etc. The rope can have a density in a range from about <NUM>/cm<NUM> (grams per centimeter cubed) to about <NUM>/cm<NUM>, about <NUM>/cm<NUM> to about <NUM>/cm<NUM>, or about <NUM>/cm<NUM> to about <NUM>/cm<NUM>.

Suitable proteins for use in embodiments described herein include, but are not limited to, collagen, gelatin, silk, and the like. In some embodiments, the protein can be a recombinant protein. As used herein, a recombinant protein means an artificially produced, and often purified, protein such as collagen, gelatin, silk, and the like.

As used herein, coating means covering a substrate with a liquid and drying, cooling, and/or curing the liquid to a solid.

As used herein, the phrase "disposed on" means that a first component (e.g., coating) is in direct contact with a second component. A first component "disposed on" a second component can be deposited, formed, placed, or otherwise applied directly onto the second component. In other words, if a first component is disposed on a second component, there are no components between the first component and the second component.

As used herein, the phrase "disposed over" means other components (e.g., coatings) may or may not be present between a first component and a second component.

As used herein "collagen" refers to the family of at least <NUM> distinct naturally occurring collagen types including, but not limited to collagen types I, II, III, IV, V, VI, VII, VIII, IX, X, XI, XII, XIII, XIV, XV, XVI, XVII, XVIII, XIX, and XX. The term collagen as used herein also refers to collagen prepared using recombinant techniques. The term collagen includes collagen, collagen fragments, collagen-like proteins, triple helical collagen, alpha chains, monomers, gelatin, trimers and combinations thereof. Recombinant expression of collagen and collagen-like proteins is known in the art (see, e.g., <CIT>, Bovine collagen and method for producing recombinant gelatin; <CIT> and <CIT>, incorporated by reference herein in their entireties) Unless otherwise specified, collagen of any type, whether naturally occurring or prepared using recombinant techniques, can be used in any of the embodiments described herein. That said, in some embodiments, the composite materials described herein can be prepared using bovine Type I collagen. Collagens are characterized by a repeating triplet of amino acids, -(Gly-X-Y)n-, so that approximately one-third of the amino acid residues in collagen are glycine. X is often proline and Y is often hydroxyproline. Thus, the structure of collagen may consist of three intertwined peptide chains of differing lengths. Different animals may produce different amino acid compositions of the collagen, which may result in different properties (and differences in the resulting leather). Collagen triple helices (also called monomers or tropocollagen) may be produced from alpha-chains of about <NUM> amino acids long, so that the triple helix takes the form of a rod of about approximately <NUM> long, with a diameter of approximately <NUM>. In the production of extracellular matrix by fibroblast skin cells, triple helix monomers may be synthesized and the monomers may self-assemble into a fibrous form. These triple helices may be held together by electrostatic interactions (including salt bridging), hydrogen bonding, Van der Waals interactions, dipole-dipole forces, polarization forces, hydrophobic interactions, and covalent bonding. Triple helices can be bound together in bundles called fibrils, and fibrils can further assemble to create fibers and fiber bundles. In some embodiments, fibrils can have a characteristic banded appearance due to the staggered overlap of collagen monomers. This banding can be called "D-banding. " The bands are created by the clustering of basic and acidic amino acids, and the pattern is repeated four times in the triple helix (D-period). (See, e.g., <NPL>)) The distance between bands can be approximately <NUM> for Type <NUM> collagen. These bands can be detected using diffraction Transmission Electron Microscope (TEM), which can be used to access the degree of fibrillation in collagen. Fibrils and fibers typically branch and interact with each other throughout a layer of skin. Variations of the organization or crosslinking of fibrils and fibers can provide strength to a material disclosed herein. In some embodiments, protein is formed, but the entire collagen structure is not triple helical. In certain embodiments, the collagen structure can be about <NUM>%, about <NUM>%, about <NUM>%, about <NUM>%, about <NUM>%, about <NUM>%, about <NUM>%, about <NUM>%, about <NUM>%, about <NUM>%, about <NUM>%, about <NUM>%, about <NUM>%, about <NUM>%, about <NUM>%, about <NUM>%, about <NUM>%, about <NUM>%, about <NUM>%, about <NUM>%, about <NUM>%, about <NUM>% or <NUM>% triple helical.

In some embodiments, the collagen can be chemically modified to promote chemical and/or physical crosslinking between the collagen fibrils. Chemical crosslinking is possible due to reactive groups such as lysine, glutamic acid, and hydroxyl groups on the collagen molecule project from collagen's rod-like fibril structure. Crosslinking that involves these reactive groups prevents the collagen molecules from sliding past each other under stress, thereby increasing the mechanical strength of the collagen fibrils. Chemical crosslinking reactions can include, for example, reactions with the ε-amino group of lysine or reaction with carboxyl groups of the collagen molecule. In some embodiments, enzymes such as transglutaminase can also be used to generate crosslinks between glutamic acid and lysine to form a stable γ-glutamyl-lysine crosslink. Inducing crosslinking between functional groups of neighboring collagen molecules is known in the art.

In some embodiments, the collagen can be crosslinked or lubricated during fibrillation. In some embodiments, the collagen can be crosslinked or lubricated after fibrillation. For example, collagen fibrils can be treated with compounds containing chromium, at least one aldehyde group, or vegetable tannins prior to network formation, during network formation, or during network gel formation.

In some embodiments, up to about <NUM> wt% of a crosslinking agent, based on total weight of a collagen solution can be used to crosslink collagen during fibrillation. For example, about <NUM> wt%, about <NUM> wt%, about <NUM> wt%, about <NUM> wt%, about <NUM> wt%, about <NUM> wt%, about <NUM> wt%, about <NUM> wt%, about <NUM> wt%, about <NUM> wt%, about <NUM> wt%, or about <NUM> wt%, or an amount of crosslinking agent within a range having any two of these values as endpoints, inclusive of the endpoints, can be used. In some embodiments, the amount of crosslinking agent can be in a range of about <NUM> wt% to about <NUM> wt%, about <NUM> wt% to about <NUM> wt%, about <NUM> wt% to about <NUM> wt%, about <NUM> wt% to about <NUM> wt%, about <NUM> wt% to about <NUM> wt%, or about <NUM> wt% to about <NUM> wt%. In some embodiments, the crosslinking agent can include tanning agents used for conventional leather. In some embodiments, the crosslinking agent can be covalently bound to the collagen fibrils. In some embodiments, the crosslinking agent can be non-covalently associated with the collagen fibrils.

Regardless of the type of collagen, all can be formed and stabilized through a combination of physical and chemical interactions including electrostatic interactions (including salt bridging), hydrogen bonding, Van der Waals interactions, dipole-dipole forces, polarization forces, hydrophobic interactions, and covalent bonding often catalyzed by enzymatic reactions. For Type I collagen fibrils, fibers, and fiber bundles, its complex assembly is achieved in vivo during development and is critical in providing mechanical support to the tissue while allowing for cellular motility and nutrient transport.

Various distinct collagen types have been identified in vertebrates, including bovine, ovine, porcine, chicken, and human collagens. Generally, the collagen types are numbered by Roman numerals, and the chains found in each collagen type are identified by Arabic numerals. Detailed descriptions of structure and biological functions of the various different types of naturally occurring collagens are generally available in the art; see, e.g., <NPL>; <NPL>; <NPL>; and <NPL>.

Type I collagen is the major fibrillar collagen of bone and skin, comprising approximately <NUM>-<NUM>% of an organism's total collagen. Type I collagen is the major structural macromolecule present in the extracellular matrix of multicellular organisms and comprises approximately <NUM>% of total protein mass. Type I collagen is a heterotrimeric molecule comprising two α1(I) chains and one α2(<NUM>) chain, encoded by the COL1A1 and COL1A2 genes, respectively. Other collagen types are less abundant than type I collagen, and exhibit different distribution patterns. For example, type II collagen is the predominant collagen in cartilage and vitreous humor, while type III collagen is found at high levels in blood vessels and to a lesser extent in skin.

Type II collagen is a homotrimeric collagen comprising three identical al(II) chains encoded by the COL2A1 gene. Purified type II collagen may be prepared from tissues by, methods known in the art, for example, by procedures described in<NPL>.

Type III collagen is a major fibrillar collagen found in skin and vascular tissues. Type III collagen is a homotrimeric collagen comprising three identical α1(III) chains encoded by the COL3A1 gene. Methods for purifying type III collagen from tissues can be found in, for example, <NPL>; and Miller and Rhodes, supra.

In certain embodiments, the collagen can be Col3 alpha. In some embodiments, the collagen can be encoded by a sequence that is about <NUM>%, about <NUM>%, about <NUM>%, about <NUM>%, about <NUM>%, about <NUM>%, about <NUM>%, about <NUM>%, or about <NUM>% identical to a naturally occurring Col3 alpha chain sequence. In other embodiments, the collagen can be encoded by a sequence that is about <NUM>%, about <NUM>%, about <NUM>%, about <NUM>%, about <NUM>%, about <NUM>%, about <NUM>%, about <NUM>%, or about <NUM>% identical to SEQ ID NO: <NUM>. In particular embodiments, the collagen is encoded by SEQ ID NO: <NUM>. Sequence identity or similarity can be determined using a similarity matrix such as BLOSUM45, BLOSUM62 or BLOSUM80 where BLOSUM45 can be used for closely related sequences, BLOSUM62 for midrange sequences, and BLOSUM80 for more distantly related sequences. Unless otherwise indicated a similarity score will be based on use of BLOSUM62. When BLASTP is used, the percent similarity is based on the BLASTP positives score and the percent sequence identity is based on the BLASTP identities score. BLASTP "Identities" shows the number and fraction of total residues in the high scoring sequence pairs which are identical; and BLASTP "Positives" shows the number and fraction of residues for which the alignment scores have positive values and which are similar to each other. Amino acid sequences having these degrees of identity or similarity or any intermediate degree of identity or similarity to the amino acid sequences disclosed herein are contemplated and encompassed by this disclosure. Typically, a representative BLASTP setting uses an Expect Threshold of <NUM>, a Word Size of <NUM>, BLOSUM <NUM> as a matrix, and Gap Penalty of <NUM> (Existence) and <NUM> (Extension) and a conditional compositional score matrix adjustment. Other common settings are known to those of ordinary skill in the art.

Type IV collagen is found in basement membranes in the form of sheets rather than fibrils. Most commonly, type IV collagen contains two α1(IV) chains and one α2(IV) chain. The particular chains comprising type IV collagen are tissue-specific. Type IV collagen may be purified using, for example, the procedures described in<NPL>.

Type V collagen is a fibrillar collagen found in, primarily, bones, tendon, cornea, skin, and blood vessels. Type V collagen exists in both homotrimeric and heterotrimeric forms. One form of type V collagen is a heterotrimer of two α1(V) chains and one α2(V) chain. Another form of type V collagen is a heterotrimer of α1(V), α2(V), and α3(V) chains. A further form of type V collagen is a homotrimer of α1(V). Methods for isolating type V collagen from natural sources can be found, for example, in <NPL>, and <NPL>.

Type VI collagen has a small triple helical region and two large non-collagenous remainder portions. Type VI collagen is a heterotrimer comprising α1(VI), α2(VI), and α3(VI) chains. Type VI collagen is found in many connective tissues. Descriptions of how to purify type VI collagen from natural sources can be found, for example, in<NPL>, and <NPL>.

Type VII collagen is a fibrillar collagen found in particular epithelial tissues. Type VII collagen is a homotrimeric molecule of three α1(VII) chains. Descriptions of how to purify type VII collagen from tissue can be found in, for example,<NPL>, and<NPL>. Type VIII collagen can be found in Descemet's membrane in the cornea. Type VIII collagen is a heterotrimer comprising two α1(VIII) chains and one α2(VIII) chain, although other chain compositions have been reported. Methods for the purification of type VIII collagen from nature can be found, for example, in <NPL>, and <NPL>.

Type IX collagen is a fibril-associated collagen found in cartilage and vitreous humor. Type IX collagen is a heterotrimeric molecule comprising α1(IX), α2(IX), and α3 (IX) chains. Type IX collagen has been classified as a FACIT (Fibril Associated Collagens with Interrupted Triple Helices) collagen, possessing several triple helical domains separated by non-triple helical domains. Procedures for purifying type IX collagen can be found, for example, in <NPL>; <NPL>; and<NPL>.

Type X collagen is a homotrimeric compound of α1(X) chains. Type X collagen has been isolated from, for example, hypertrophic cartilage found in growth plates. (See, e.g., <NPL>.

Type XI collagen can be found in cartilaginous tissues associated with type II and type IX collagens, and in other locations in the body. Type XI collagen is a heterotrimeric molecule comprising α1(XI), α2(XI), and α3(XI) chains. Methods for purifying type XI collagen can be found, for example, in Grant et al.

Type XII collagen is a FACIT collagen found primarily in association with type I collagen. Type XII collagen is a homotrimeric molecule comprising three α1(XII) chains. Methods for purifying type XII collagen and variants thereof can be found, for example, in <NPL>; <NPL>; and<NPL>.

Type XIII is a non-fibrillar collagen found, for example, in skin, intestine, bone, cartilage, and striated muscle. A detailed description of type XIII collagen may be found, for example, in <NPL>.

Type XIV is a FACIT collagen characterized as a homotrimeric molecule comprising α1(XIV) chains. Methods for isolating type XIV collagen can be found, for example, in <NPL>,and Watt et al.

Type XV collagen is homologous in structure to type XVIII collagen. Information about the structure and isolation of natural type XV collagen can be found, for example, in <NPL>; <NPL>; <NPL>; and <NPL>.

Type XVI collagen is a fibril-associated collagen, found, for example, in skin, lung fibroblast, and keratinocytes. Information on the structure of type XVI collagen and the gene encoding type XVI collagen can be found, for example, in <NPL>; and <NPL>.

Type XVII collagen is a hemidesmosal transmembrane collagen, also known at the bullous pemphigoid antigen. Information on the structure of type XVII collagen and the gene encoding type XVII collagen can be found, for example, in<NPL>; and <NPL>.

Type XVIII collagen is similar in structure to type XV collagen and can be isolated from the liver. Descriptions of the structures and isolation of type XVIII collagen from natural sources can be found, for example, in <NPL>; <NPL>; <NPL>; and <NPL>.

Type XIX collagen is believed to be another member of the FACIT collagen family, and has been found in mRNA isolated from rhabdomyosarcoma cells. Descriptions of the structures and isolation of type XIX collagen can be found, for example, in <NPL>; <NPL>; and <NPL>).

Type XX collagen is a newly found member of the FACIT collagenous family, and has been identified in chick cornea. (See, e.g., <NPL>; and<NPL>.

Any type of collagen, truncated collagen, unmodified or post-translationally modified, or amino acid sequence-modified collagen that can be fibrillated and crosslinked by the methods described herein can be used to produce a collagen-containing layer (e.g., collagen/polymer matrix layer) as described herein. The degree of fibrillation of the collagen molecules can be determined via x-ray diffraction. This characterization will provide d-spacing values which will correspond to different periodic structures present (e.g., <NUM> spacing vs. amorphous). In some embodiments, the collagen can be substantially homogenous collagen, such as only Type I or Type III collagen or can contain mixtures of two or more different kinds of collagens. In embodiments, the collagen is recombinant collagen.

For example, a collagen composition can homogenously contain a single type of collagen molecule, for example <NUM>% bovine Type I collagen or <NUM>% Type III bovine collagen, or can contain a mixture of different kinds of collagen molecules or collagen-like molecules, such as a mixture of bovine Type I and Type III molecules. The collagen mixtures can include amounts of each of the individual collagen components in the range of about <NUM>% to about <NUM>%, including subranges. For example, the amounts of each of the individual collagen components within the collagen mixtures can be about <NUM>%, about <NUM>%, about <NUM>%, about <NUM>%, about <NUM>%, about <NUM>%, about <NUM>%, about <NUM>%, about <NUM>%, about <NUM>%, or about <NUM>%, or within a range having any two of these values as endpoints. For example, in some embodiments, a collagen mixture can contain about <NUM>% Type I collagen and about <NUM>% Type III collagen. Or, in some embodiments, a collagen mixture can contain about <NUM>% of Type I collagen, about <NUM>% of Type II collagen, and about <NUM>% of Type III collagen, where the percentage of collagen is based on the total mass of collagen in the composition or on the molecular percentages of collagen molecules.

In some embodiments, the collagen can be plant-based collagen. For example, the collagen can be a plant-based collagen made by CollPlant.

In some embodiments, a collagen solution can be fibrillated into collagen fibrils. As used herein, collagen fibrils refer to nanofibers composed of tropocollagen or tropocollagen-like structures (which have a triple helical structure). In some embodiments, triple helical collagen can be fibrillated to form nanofibrils of collagen. To induce fibrillation, the collagen can be incubated to form the fibrils for a time period in the range of about <NUM> minute to about <NUM> hours, including subranges. For example, the collagen can be incubated for about <NUM> minute, about <NUM> minutes, about <NUM> minutes, about <NUM> minutes, about <NUM> minutes, about <NUM> minutes, about <NUM> minutes, about <NUM> hour, about <NUM> hours, about <NUM> hours, about <NUM> hours, about <NUM> hours, about <NUM> hours, about <NUM> hours, about <NUM> hours, about <NUM> hours, about <NUM> hours, about <NUM> hours, about <NUM> hours, about <NUM> hours, about <NUM> hours, about <NUM> hours, about <NUM> hours, about <NUM> hours, about <NUM> hours, about <NUM> hours, about <NUM> hours, about <NUM> hours, about <NUM> hours, about <NUM> hours, or about <NUM> hours, or within a range having any two of these values as endpoints, inclusive of the endpoints. In some embodiments, the collagen can be incubated for about <NUM> minutes to about <NUM> hours, about <NUM> minutes to about <NUM> hours, about <NUM> minutes to about <NUM> hours, about <NUM> minutes to about <NUM> hours, about <NUM> minutes to about <NUM> hours, about <NUM> minutes to about <NUM> hours, about <NUM> hour to about <NUM> hours, about <NUM> hours to about <NUM> hours, about <NUM> hours to about <NUM> hours, about <NUM> hours to about <NUM> hours, about <NUM> hours to about <NUM> hours, about <NUM> hours to about <NUM> hours, about <NUM> hours to about <NUM> hours, or about <NUM> hours to about <NUM> hours.

In some embodiments, the collagen fibrils can have an average diameter in the range of about <NUM> (nanometer) to about <NUM> (micron, micrometer), including subranges. For example, the average diameter of the collagen fibrils can be about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, or about <NUM>, or within a range having any two of these values as endpoints, inclusive of the endpoints. In some embodiments, the average diameter can be in a range of about <NUM> to about <NUM>, about <NUM> to about <NUM>, about <NUM> to about <NUM>, about <NUM> to about <NUM>, about <NUM> to about <NUM>, about <NUM> to about <NUM>, about <NUM> to about <NUM>, about <NUM> to about <NUM>, about <NUM> to about <NUM>, about <NUM> to about <NUM>, or about <NUM> to about <NUM>.

In some embodiments, an average length of the collagen fibrils is in the range of about <NUM> to about <NUM> (millimeter), including subranges. For example, the average length of the collagen fibrils can be about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, or about <NUM>, or within a range having any two of these values as endpoints, inclusive of the endpoints. In some embodiments, the average length can be in a range of about <NUM> to about <NUM>, about <NUM> to about <NUM>, about <NUM> to about <NUM>, about <NUM> to about <NUM>, about <NUM> to about <NUM>, about <NUM> to about <NUM>, about <NUM> to about <NUM>, about <NUM> to about <NUM>, about <NUM> to about <NUM>, about <NUM> to about <NUM>, about <NUM> to about <NUM>, about <NUM> to about <NUM>, about <NUM> to about <NUM>, or about <NUM> to about <NUM>.

In some embodiments, the collagen fibrils can exhibit a unimodal, bimodal, trimiodal, or multimodal distribution. For example, a collagen-containing layer can include two different fibril preparations, each having a different range of fibril diameters arranged around one of two different modes. Such collagen mixtures can be selected to impart additive, synergistic, or a balance of physical properties to the collagen-containing layer.

In some embodiments, the collagen fibrils form networks. For example, individual collagen fibrils can associate to exhibit a banded pattern. These banded fibrils can then associate into larger aggregates of fibrils. However, in some embodiments, the fibrillated collagen can lack a higher order structure. For example, the collagen fibrils can be unbundled and provide a strong and uniform non-anisotropic structure to layered collagen materials. In other embodiments, the collagen fibrils can be bundled or aligned into higher order structures. For example, the collagen fibrils can have an orientation index in the range of <NUM> to about <NUM>, including subranges. For example, the orientation index of the collagen fibrils can be <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, or about <NUM>, or within a range having any two of these values as endpoints, inclusive of the endpoints, inclusive of the endpoints. In some embodiments, the orientation index can be in a range of about <NUM> to about <NUM>, about <NUM> to about <NUM>, about <NUM> to about <NUM>, or about <NUM> to about <NUM>. An orientation index of <NUM> describes collagen fibrils that are perpendicular to other fibrils, and an orientation index of <NUM> describes collagen fibrils that are completely aligned.

Embodiments of the present disclosure provide materials, and methods of making materials, that have a look and feel, as well as mechanical properties, similar to natural leather. The materials can have, among other things, haptic properties, aesthetic properties, mechanical/performance properties, manufacturability properties, and/or thermal properties similar to natural leather. Mechanical/performance properties that can be similar to natural leather include, but are not limited to, tensile strength, tear strength, elongation at break, resistance to abrasion, internal cohesion, water resistance, breathability, and the ability to retain color when rubbed. Haptic properties that can be similar to natural leather include, but are not limited to, softness, rigidity, coefficient of friction, and compression modulus. Aesthetic properties that can be similar to natural leather include, but are not limited to, dyeability, embossability, aging, color, color depth, and color patterns. Manufacturing properties that can be similar to natural leather include, but are not limited to, the ability to be stitched, cut, skived, and split. Thermal properties that can be similar to natural leather include, but are not limited to, heat resistance and resistance to stiffening or softening over a significantly wide temperature range, for example <NUM> to <NUM>.

In some embodiments, materials described herein can include one or more fatliquors. Fatliquor may be incorporated into a material using a "lubricating" and "fatliquoring" process. Exemplary fatliquors include, but are not limited to, fats, oils, including biological oils such as cod oil, mineral oils, or synthetic oils such as sulfonated oils, polymers, organofunctional siloxanes, or other hydrophobic compounds or agents used for fatliquoring conventional leather, or mixtures thereof. Other fatliquors can include surfactants such as anionic surfactants, cationic surfactants, cationic polymeric surfactants, anionic polymeric surfactants, amphiphilic polymers, fatty acids, modified fatty acids, nonionic hydrophilic polymers, nonionic hydrophobic polymers, poly acrylic acids, poly methacrylic acids, acrylics, natural rubbers, synthetic rubbers, resins, amphiphilic anionic polymers and copolymers, amphiphilic cationic polymer and copolymers and mixtures thereof as well as emulsions or suspensions of these in water, alcohol, ketones, and other solvents. One or more fatliquors can be incorporated in any amount that facilitates movement of collagen fibrils, or that confers leather-like properties such as flexibility, decrease in brittleness, durability, or water resistance. In some embodiments, the fatliquor may be TRUPOSOL® BEN, an acrylic acid based retanning polymer available from Trumpler.

In some embodiments, materials described herein can be tanned. Tanning can be performed in any number of well-understood ways, including by contacting a material with a vegetable tanning agent, blocked isocyanate compounds, chromium compound, aldehyde, syntan, natural resin, tanning natural oil, or modified oil. Blocked isocyanate compounds can include X-tan. Vegetable tannins can include pyrogallol- or pyrocatechin-based tannins, such as valonea, mimosa, ten, tara, oak, pinewood, sumach, quebracho, and chestnut tannins. Chromium tanning agents can include chromium salts such as chromium sulfate. Aldehyde tanning agents can include glutaraldehyde and oxazolidine compounds. Syntans can include aromatic polymers, polyacrylates, polymethacrylates, copolymers of maleic anhydride and styrene, condensation products of formaldehyde with melamine or dicyandiamide, lignins, and natural flours.

In some embodiments, after tanning, a material can be retanned. Retanning refers to post-tanning treatments. Such treatments can include tanning a second time, wetting, sammying, dehydrating, neutralization, adding a coloring agent such as a dye, fat liquoring, fixation of unbound chemicals, setting, conditioning, softening, and/or buffing.

In some embodiments, materials decried herein can be colored with a coloring agent. In some embodiments the coloring agent can be a dye, for example an acid dye, a fiber reactive dye, a direct dye, a sulfur dye, a basic dye, or a reactive dye. In some embodiments, the coloring agent can be pigment, for example a lake pigment.

A fiber reactive dye includes one or more chromophores that contain pendant groups capable of forming covalent bonds with nucleophilic sites in fibrous, cellulosic substrates in the presence of an alkaline pH and raised temperature. These dyes can achieve high wash fastness and a wide range of brilliant shades. Exemplary fiber reactive dyes, include but are not limited to, sulphatoethylsulphone (Remazol), vinyl sulphone, and acrylamido dyes. These dyes can dye protein fibers such as silk, wool and nylon by reacting with fiber nucleophiles via a Michael addition. Direct dyes are anionic dyes capable of dying cellulosic or protein fibers. In the presence of an electrolyte such as sodium chloride or sodium sulfate, near boiling point, these dyes can have an affinity to cellulose. Exemplary direct dyes include, but are not limited to, azo, stilbene, phthalocyanine, and dioxazine.

In some embodiments, the materials described herein can be, or can be made into, a medical device, for example an implantable scaffold.

Embodiments described herein can use sheets, textile, ropes, fibers, strands, and yarns that can be coated. Fibers can be natural, synthetic, or combinations thereof. Examples of natural fibers include, but are not limited to, wool, silk, cotton, bamboo, and the like. Examples of manufactured fibers include, but are not limited to, glass, polyester, rayon, acrylic, nylon, carbon fiber, glass and the like.

In some embodiments, fibers can be carded to align the fibers, processed into roving, spun into strands, and two or more strands can be plied into yarns. Yarns can be made from a single strand of fibers to any number of strands that are plied together.

A core sheath material contains a central portion (core) made from one or more materials and a surrounding portion (sheath) made from a second material. The core can be a fiber or a yarn. The sheath can be a polymer or any material that can coat the core. Examples are collagen, gelatin, silk protein, or any other polymers that can be coagulated by the pretreatment, and combinations thereof.

In some embodiments, core sheath fibers can be made by dipping or coating fibers or yarns through a polymer bath or a spinneret that extrudes a polymer solution, dispersion, paste or melt and the like. The fiber or yarn becomes a core surrounded by the sheath, which is a coating.

Substrates such as a sheet, a textile, a fiber, a strand or a yarn can be coated with a solution by spraying, dipping, stirring, extruding, or other methods known in the art. Suitable textiles can be comprised of wool, silk, cotton, bamboo, glass, polyester, rayon, acrylic, nylon, carbon, and the like, as well as combinations of any of the foregoing. Suitable textile constructions can be woven, knitted, crocheted, knotted, felted, dry-laid, wet-laid, spun-bonded, spun-lace, melt-blown, spunmelt, needlepunched and the like. Suitable sheets can be films or foams made of polymers such as acetate, nylon, mylar, polyethylene, polyurethane, vinyl, cellophane, and the like. Additionally, other substrates that can be coated are brick, metal, ceramic, plastic, glass, rubber, wood, and the like.

In some embodiments, the solution for coating the substrate can contain a material that coagulates proteins onto the substrate. Suitable materials include but are not limited to salts, polymers that are not miscible with the protein, pH adjusting agents, non-solvents for the protein (liquids that do not dissolve the protein) and the like. Suitable salts include, but are not limited to, sodium sulfate, calcium chloride, sodium chloride, and the like. Suitable pH adjusting agents include, but are not limited to, hydrochloric acid, acetic acid, citric acid, sodium hydroxide, potassium hydroxide, and the like. In some embodiments, a change in pH can bring the protein being used to coat the substrate to its isoelectric point causing the protein to coagulate. Suitable non-solvents include, but are not limited to, acetone, ethyl acetate, and the like. Additionally or alternatively, a change in temperature can be used to coagulate proteins onto the substrate. Suitable temperatures can be less than room temperature, for example less than about <NUM>, less than about <NUM>, less than about <NUM>, or less than about <NUM>. In some embodiments, the temperature can be less than any of these temperature and equal to or greater than <NUM>. For example, a collagen solution can be warmed to <NUM>, a chilled yarn (at <NUM>) can then be dipped into the warmed collagen solution, and the collagen around the chilled yarn can be cooled such that the protein coagulates onto the yarn.

In some embodiments, the substrate can be coated with a salt solution, dried and coated with a protein. In some embodiments, the salt coating can be disposed over the substrate. In some embodiments, the salt coating can be disposed on the substrate. Suitable salts, as recited above, include, but are not limited to, sodium sulfate, calcium chloride, sodium chloride, and the like.

The salt solution can be made by dissolving one or more salts in a solvent. Suitable solvents include, but are not limited to, water, ethanol/water, glycol such as propylene glycol and dipropylene glycol, glycerin, and any other solvents that can dissolve salts. Suitable salt solutions include saturated salt solutions. The concentration of the salt in a saturated solution will depend on the solvent, the salt used, and the temperature at which the salt is dissolved. The substrate can be stirred in the salt solution, removed, and dried to create a salt solution coated substrate. Suitable stirring or dipping times can range from about <NUM> seconds to about <NUM> minutes, about <NUM> seconds to about <NUM> minute, or about <NUM> minute to about <NUM> minutes, or within a range having any two of these values as endpoints, inclusive of the endpoints. Alternatively, the salt solution can be sprayed onto the substrate and dried. Suitable drying methods can include ovens, air drying, tunnel drying, and the like. Suitable drying times can range from about <NUM> seconds to overnight (about <NUM> hours) or about <NUM> seconds to about <NUM> minutes. The amount of salt coated onto the substrate can range from about <NUM>% to about <NUM>%, about <NUM>% to about <NUM>%, about <NUM>% to about <NUM>%, about <NUM>% to about <NUM>%, about <NUM>% to about <NUM>%, or about <NUM>% to about <NUM>% based on the weight of the substrate before and after coating, or within a range having any two of these values as endpoints, inclusive of the endpoints.

In some embodiments, proteins such as collagen, gelatin, silk, and the like can be dissolved or suspended in a liquid to create a protein solution. Suitable liquids include, but are not limited to, water, methanol, ethanol, acetic acid, and the like. The concentration of the protein in the solution or dispersion can range from about <NUM>% to about <NUM>%, about <NUM>% to about <NUM>%, or about <NUM>% to about <NUM>% based on total weight of the solution or dispersion, or within a range having any two of these values as endpoints, inclusive of the endpoints.

In some embodiments, a salt-coated substrate can be coated with the protein solution by stirring or dipping in the solution and drying the coated substrate. Suitable stirring or dipping times can range from about <NUM> seconds to <NUM> minutes, about <NUM> seconds to about <NUM> minute, or about <NUM> minute to about <NUM> minutes. Suitable drying times can range from about <NUM> seconds to overnight, about <NUM> seconds to about <NUM> minutes, about <NUM> minutes to about <NUM> hours, or about <NUM> hour to about <NUM> hours, or within a range having any two of these values as endpoints, inclusive of the endpoints. In some embodiments, the protein coating can be disposed over the salt coating. In some embodiments, the protein coating can be disposed on the salt coating.

In some embodiments, the amount of protein coated onto the substrate can range from about <NUM>% to about <NUM>%, about <NUM>% to about <NUM>%, about <NUM>% to about <NUM>%, about <NUM>% to about <NUM>%, or about <NUM>% to about <NUM>% based on the weight of the substrate before and after coating, or within a range having any two of these values as endpoints, inclusive of the endpoints.

In some embodiments, the protein-coated substrate (for example a coated fiber) can be coated with additional layers. For example, the protein-coated substrate can be coated with additional layers for ease of processing or abrasion resistance. Additional layers can be the same protein, a different protein, or a polymeric material without a protein. Suitable polymeric materials include, but are not limited to, polyurethanes, polyacrylates, polyvinylchloride, and the like. The additional layers can contain the same protein or different protein(s) relative to the coating layer, or with respect to subsequent layers. Additional layers can number from <NUM> to <NUM>, <NUM> to <NUM>, <NUM> to <NUM>, <NUM> to <NUM>, or <NUM> to <NUM>, alternative minimum values include <NUM>, <NUM>, <NUM>, or <NUM> layers. In some embodiments, the additional layer(s) can contain no protein.

In some embodiments, the substrate can be coated with a polymer, prior to coating with a protein. In particular embodiments, the polymer is immiscible with the protein. In certain embodiments, the polymer can be applied to the substrate using a solution or suspension of the polymer. Suitable protein immiscible polymers include, but are not limited to, polyurethanes such as SANCURE™ <NUM> and Hauthaway L2985, and other polymers that are not miscible with the protein of a protein coating. In some embodiments, the polymer coating can be disposed over the substrate. In some embodiments, the polymer coating can be disposed on the substrate.

The polymer solution or suspension can be made by dissolving, dispersing, or diluting the polymer in a solvent. Suitable solvents include, but are not limited to, water, ethanol, and the like. The concentration of the polymer in solution or suspension can range from about <NUM>% to about <NUM>%, about <NUM>% to about <NUM>%, about <NUM>% to about <NUM>%, or about <NUM>% to about <NUM>% based on total weight of the solution or suspension, , or within a range having any two of these values as endpoints, inclusive of the endpoints. The substrate can be stirred or dipped in the polymer solution or suspension and removed to create a polymer solution or suspension coated substrate. Suitable stirring or dipping times can range from about <NUM> seconds to about <NUM> minutes, about <NUM> seconds to about <NUM> minute, or about <NUM> minute to about <NUM> minutes. Alternatively, the polymer solution or suspension can be sprayed onto the substrate. The amount of polymer coated onto the substrate can range from about <NUM>% to about <NUM>%, about <NUM>% to about <NUM>%, about <NUM>% to about <NUM>%, about <NUM>% to about <NUM>%, about <NUM>% to about <NUM>%, or about <NUM>% to about <NUM>% based on the weight of the substrate before and after coating, or within a range having any two of these values as endpoints, inclusive of the endpoints.

Proteins such as those recited above including collagen, gelatin, silk, and the like can be dissolved or suspended in a liquid to create a protein solution. Suitable liquids include, but are not limited to, water, methanol, ethanol, and combinations thereof. The concentration of the protein in the solution or dispersion can range from about <NUM>% to about <NUM>%, about <NUM>% to about <NUM>%, or about <NUM>% to about <NUM>% based on the total weight of the solution or dispersion, or within a range having any two of these values as endpoints, inclusive of the endpoints.

In some embodiments, the polymer solution-coated substrate can be coated with the protein solution by stirring or dipping in the solution and subsequently dried. In some embodiments, the protein coating can be disposed over the polymer coating. In some embodiments, the protein coating can be disposed on the polymer coating.

Suitable stirring or dipping times can range from about <NUM> seconds to about <NUM> minutes, about <NUM> seconds to about <NUM> minute, or about <NUM> minute to about <NUM> minutes, or within a range having any two of these values as endpoints, inclusive of the endpoints. Suitable drying times can range from about <NUM> seconds to overnight, about <NUM> seconds to about <NUM> minutes, about <NUM> minutes to about <NUM> hours, or about <NUM> hour to about <NUM> hours, or within a range having any two of these values as endpoints, inclusive of the endpoints. The amount of protein coated onto the substrate can range from about <NUM>% to about <NUM>%, about <NUM>% to about <NUM>%, about <NUM>% to about <NUM>%, about <NUM>% to about <NUM>%, about <NUM>% to about <NUM>%, or about <NUM>% to about <NUM>% based on the weight of the substrate before and after coating, or within a range having any two of these values as endpoints, inclusive of the endpoints.

In some embodiments, a substrate can be coated with a protein coating by fibrillating a protein over the substrate. In some embodiments, a substrate can be coated with a protein coating by fibrillating a protein directly on the substrate.

In some embodiments, to promote fibrillation of a protein on a substrate, the pH of the protein solution can be raised by adding a buffer or adjusting a salt concentration of the solution. In some embodiments, the pH can be raised at a temperature below about <NUM>, for example at a temperature in a range of about <NUM> to about <NUM>. In some embodiments, fibrillation can be facilitated by including a nucleating agent. Salts used for fibrillation can include phosphate salts and chloride salts, such as Na<NUM>PO<NUM> (trisodium phosphate), K<NUM>PO<NUM> (tripotassium phosphate), KCl (potassium chloride), and NaCl (sodium chloride). Additional exemplary salts include any conjugate salt of an acid such as a sulfate, a phosphate, a chloride, an acetate, a nitrate and a citrate. The salt concentration during fibrillation can be in the range of about <NUM> to about <NUM>, including subranges. For example, the salt concentration can be about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, or about <NUM>, or within a range having any two of these values as endpoints, inclusive of the endpoints. The acids, salt concentration, salt type, pH, temperature, and collagen concentration for a fibrillation step affects how fast fibrils are formed.

Is some embodiments, the pH of the collagen solution can be adjusted to a pH in a range of about <NUM> to about <NUM>. In some embodiments, the pH of the collagen solution can be adjusted to a pH in a range of about <NUM> to about <NUM>. In some embodiments, the pH of the collagen solution can be adjusted to a pH in a range of about <NUM> to about <NUM>. In some embodiments, the pH of the collagen solution can be adjusted to a pH of about <NUM>, about <NUM>, or greater. In some embodiments, the pH can be adjusted to a range of about <NUM> to about <NUM>, a range of about <NUM> to about <NUM>, or a range of about <NUM> to about <NUM>. In some embodiments, the salt concentration and pH can be simultaneously adjusted to induce or promote fibrillation. In some embodiments, the temperature is about <NUM> or below while adjusting the pH and/or adding the salt solution. In certain embodiments, the temperature is below about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM> , about <NUM>, about <NUM>, about <NUM>, or about <NUM> while adjusting the pH and/or adding the salt solution. In some embodiments, after adjusting the pH of the collagen solution to within an appropriate range, fibrillation can be conducted at a temperature in a range of between about <NUM> and about <NUM>, between about <NUM> and about <NUM>, between about <NUM> and about <NUM>, between about <NUM> and about <NUM>, or between about <NUM> and about <NUM>. In certain embodiments, the temperature is about <NUM>, about <NUM> , about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM> , about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, or about <NUM> during fibrillation.

Some embodiments described herein are directed to a protein-coated substrate, wherein the substrate is selected from the group consisting of a sheet, a textile, a rope, a fiber, a strand, and a yarn. Proteins such as collagen, gelatin, silk, and the like can be coated onto the substrate as described herein. In some embodiments, fibers can be coated with a protein as described above, then carded into slivers, and spun into yarn. In some embodiments, fibers can be processed into a yarn through these processing steps: (<NUM>) "Carding" partially aligns fibers and forms them into a thin web that's brought together as a soft, very weak rope of fibers about wrist-thick with a very light twist, called "roving. " (<NUM>) The roving is then "drawn", which is a process that increases the parallelism of the fibers and thins the web into a thinner variant of roving called a "sliver". (<NUM>) The sliver is then spun into yarn.

In some embodiments, uncoated, carded slivers can be coated with the protein, then spun into yarn. In some embodiments, coated, carded slivers can be spun into yarn and the yarn is then coated with the protein. In some embodiments, uncoated yarn can be coated with the protein.

In some embodiments, a batch of fibers can be coated with a protein, another batch of the fibers can be coated with a second protein, the two batches of fibers can be carded separately into carded slivers, and then the carded slivers can be drawn together into one blended drawn sliver that is then spun into yarn. In some embodiments, one sliver(s) or potion(s) can be coated with a protein, another sliver(s) or portion(s) can be coated with a second protein, the slivers or portions can be separately spun into single yarns and then plied together in any combination, with an unlimited number of single yarns, to form a ply-yarn.

Some embodiments are directed to protein-coated yarn that is made from a substrate selected from the group consisting of protein-coated fibers and protein-coated strands. In some embodiments, protein-coated fibers and/or protein-coated yarns can be combined with uncoated fibers and/or uncoated yarns to form a composite material.

In some embodiments, a coaxial die having concentric orifices with at least one inner orifice and one outer orifice can used to coat rope, fiber, yarns, and/or threads. In such embodiments, the rope, fiber, yarn, and/or thread can pass through the inner orifice and a liquid can pass through the outer orifice. In some embodiments, a motor can be used to drive a take up wheel to pull the rope, fiber, yarn, and/or thread through the inner orifice. In some embodiments, a pump or an extruder can be used to push the liquid through the outer orifice, thereby coating the rope, fiber, yarn, and/or thread as it exits the inner orifice. Suitable pumps include, but are not limited to, gear pumps, peristaltic pumps, syringe pumps, and the like. Suitable extruders include twin-screw extruders and the like.

In some embodiments, the liquid can be a protein solution or dispersion. Proteins such as collagen, gelatin, silk, and the like can be used. The concentration of the protein in the solution or dispersion can range from about <NUM>% to about <NUM>%, about <NUM>% to about <NUM>%, about <NUM>% to about <NUM>%, or about <NUM>% to about <NUM>% based on total weight of the solution or dispersion, or within a range having any two of these values as endpoints, inclusive of the endpoints.

In some embodiments, one or more plasticizers such as glycerol, diethylene glycol, propylene glycol, dipropylene glycol, triaectin, and the like can be combined with the protein solution or dispersion. The amount of plasticizer by weight combined with the protein solution or dispersion can range from about <NUM>% to about <NUM>%, about <NUM>% to about <NUM>%, about <NUM>% to about <NUM>%, about <NUM>% to about <NUM>%, about <NUM>% to about <NUM>%, or about <NUM>% to about <NUM>%, or within a range having any two of these values as endpoints, inclusive of the endpoints.

In some embodiments, one or more crosslinkers such as poly(ethylene glycol) diglycidyl ether, gluteraldehyde, and the like can be added to the protein solution or dispersion. The amount of crosslinker by weight combined with the protein solution or dispersion can range from about <NUM>% to about <NUM>%, about <NUM>% to about <NUM>%, about <NUM>% to about <NUM>%, about <NUM>% to about <NUM>%, about <NUM>% to about <NUM>%, about <NUM>% to about <NUM>%, or about <NUM>% to about <NUM>%, or within a range having any two of these values as endpoints, inclusive of the endpoints.

In some embodiments, two coaxial dies can be used. The first coaxial die can be used to coat the rope, fiber, yarn, and/or thread with a first coating and the second coaxial die can be used to coat the rope, fiber, yarn, and/or thread with a second coating. In some embodiments, the first coating can be a salt solution. In some embodiments, the first coating can be a solution or suspension of a polymer that is immiscible with the protein in the second coating. The second coating can be a protein solution as described herein.

Some embodiments are directed to a sheet material including entangled protein core sheath fibers, as well as methods of entangling protein core sheath fibers to form a sheet material. A "protein core sheath fiber" is a fiber including a first core composed of one or more materials coated with a protein coating as described herein.

In some embodiments, the fibers can be entangled using hydroentanglement, which uses water jets. In some embodiments, the fibers can be air entangled, which is similar to hydroentanglement, except air is used in the place of water. In some embodiments, the fibers can be needlepunched. Needlepunching is a method for entangling fibers wherein a web of material is entangled by pushing needles having barbs sized to capture fibers, pushed down into the web and pulled back up into the web. In some embodiments, spunlacing (which is similar to hydroentanglement, using water jets to make lace like hydroentangled materials) can be used.

Some embodiments are directed to methods of forming a sheet material with a mixture of protein core sheath fibers and additional fibers. The mixture of fibers can be formed into a web, which advances through fine jets of water at high pressure directed onto the web so they penetrate deeply and hydroentangle the protein core sheath fibers and the additional fibers as described herein.

Some embodiments are directed to a sheet material including protein core sheath fibers and additional fibers wherein the protein fibers and additional fibers are entangled. Some embodiments, are directed to methods of entangling protein core sheath fibers and additional fibers to form a sheet material.

As used herein additional fibers can be made from any suitable material including, but not limited to, cellulose, wood fibers, rayon, lyocell, viscose, antimicrobial yarn, SORBTEK®, nylon, polyester, elastomers such as LYCRA®, spandex or elastane and other polyester-polyurethane copolymers, carbon fibers, nonwovens, natural, synthetic, recombinant proteins, composite recombinant collagen, collagen-like protein, and combinations thereof.

Some embodiments are directed to composite collagen fiber material and methods of making the same. Composite collagen fiber material as used herein means a fiber material formed of collagen and additional fiber. In some embodiments, while in solution, collagen and additional fibers are blended and then formed into a composite collagen fiber material. The additional fibers can have lengths of about <NUM> inch, about <NUM> inch, about <NUM> inch, about <NUM> inch, about <NUM> inch, or about <NUM> inch, or any length that is suitable for forming entangled webs. In some embodiments, the composite collagen fibers can be cut to any length in the range of about <NUM> inch to about <NUM> inches or any intermediate range defined by the values recited above as upper or lower limits.

In some embodiments, the additional fibers can have diameters ranging from about <NUM> (micron, micrometer) to about <NUM>, including about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, about <NUM>, or within a range having any two of these values as endpoints, inclusive of the endpoints.

In some embodiments, the additional fibers can be mixed with collagen fibers to form a web. The amount of collagen fibers in the web can range from about <NUM>% to about <NUM>% by weight based on the total weight of the web, including about <NUM>%, about <NUM>%, about <NUM>%, about <NUM>%, about <NUM>%, about <NUM>%, about <NUM>%, about <NUM>%, or within a range having any two of these values as endpoints, inclusive of the endpoints. In some embodiments, the amount of additional fibers can range from <NUM>% to about <NUM>%, including about <NUM>%, about <NUM>%, about <NUM>%, about <NUM>%, about <NUM>%, about <NUM>%, about <NUM>%, about <NUM>%, about <NUM>%, about <NUM>% by weight based on the total weight of the web, or within a range having any two of these values as endpoints, inclusive of the endpoints.

Some embodiments are directed to a sheet material including protein core sheath fibers, wherein the protein core sheath fibers are interwoven, as well as methods of making such a sheet material, wherein the method includes weaving protein core sheath fibers together to form a woven sheet material.

Some embodiments are directed to a sheet material including protein core sheath fibers and additional fibers, wherein the collagen fibers and additional fibers are interwoven, as well as methods of making such a sheet material, wherein the method includes weaving protein core sheath fibers and additional fibers together to form a woven sheet material.

Some embodiments are directed to methods of forming a sheet material from a mixture of fibers including protein core sheath fibers and additional fibers. In such embodiments, the methods can include the steps of: forming the fibers into a web and subjecting the web to an entanglement process to entangle the protein core sheath fibers with the additional fibers. The entanglement of fibers can include a method selected from hydroentanglement, air entanglement, needle punching, and spunlacing. In a certain embodiment, the entanglement can be accomplished through hydroentanglement. Hydroentanglement is a well-known binderless process of bonding fibers together. It operates through a process that entangles individual fibers within a web by the use of high-energy water jets. Fibrous webs are passed under specially designed manifold heads with closely spaced holes which direct water jets at high pressures. Suitable pressures include pressures from about <NUM> MPa (megapascals) to about <NUM> MPa, from about <NUM> MPa to about <NUM> MPa, from about <NUM> MPa to about <NUM> MPa, or from about <NUM> MPa to about <NUM> MPa. The energy imparted by these water jets moves and rearranges the fibers in the web in a multitude of directions. As the fibers escape the pressure of the water streams, they move in any direction of freedom available. In the process of moving, they entangle with one another providing significant bonding strength to the fibrous webs, without the use of chemical bonding agents.

Some embodiments are directed to methods of forming sheet material with a mixture of protein core sheath fibers and additional fibers. The mixture of fibers can be formed into a web, which advances through fine jets of water at high pressure directed onto the web so they penetrate deeply and hydroentangle the protein core sheath fibers. The formed sheet material can be similar in both chemistry and structure to the corium layer of leather.

Some embodiments are directed to methods of forming a leather-like material with a grain layer and a corium layer including providing a formed sheet material according to an embodiment as described herein, providing a concentrate of protein, applying the concentrate onto the formed sheet material, rolling the concentrate onto the formed sheet material, dewatering the material, and pressing the material in a heated press. As used herein, a concentrate means a solution containing from about <NUM>% to about <NUM>% of a protein based on the total weight of the solution.

In some embodiments, protein-coated fibers or yarns described herein can used to prepare a structured textile by knitting, weaving, braiding, or knotting either by themselves or with other fibers or yarns. Suitable fibers can be wool, silk, cotton, bamboo, glass, polyester, rayon, acrylic, nylon, carbon, glass and the like. Suitable yarns can be natural and manufactured yarns. For example, protein-coated fibers can be in the warp direction of the textile and silk fibers are in the weft direction of the textile.

The above description provides a manner and process of making and using embodiments described herein such that any person skilled in this art is enabled to make and use the same, this enablement being provided in particular for the subject matter of the appended claims, which make up a part of the original description.

As used herein, the phrases "selected from the group consisting of," "chosen from," and the like include mixtures of the specified materials.

Where a numerical limit or range is stated herein, the endpoints are included. Also, all values and subranges within a numerical limit or range are specifically included as if explicitly written out.

The above description is presented to enable a person skilled in the art to make and use the embodiments described herein, and is provided in the context of a particular application and its requirements. Various modifications to the preferred embodiments will be readily apparent to those skilled in the art, and the generic principles defined herein can be applied to other embodiments and applications.

The embodiments discussed herein will be further clarified in the following examples.

A saturated sodium sulfate solution was prepared by dissolving <NUM> (grams) of anhydrous sodium sulfate into <NUM> (milliliters) de-ionized water and stirred at <NUM> rpm (rotations per minute) for <NUM> hour at room temperature (about <NUM>). Precipitation of extra sodium sulfate from the solution was removed by centrifuge. A pre-weighed silk yarn (Dharma Trading Co. , tussah silk, <NUM>-ply light, sport weight) was dipped into the saturated sodium sulfate solution with slight stirring for <NUM> minutes. The soaked yarn was then taken out from the salt solution. After removing excess liquid, the yarn was dried in an oven at <NUM> overnight.

A gelatin solution was made by dissolving <NUM> of gelatin (animal extract, Sigma Aldrich) into <NUM> de-ionized water and stirred at <NUM> rpm for <NUM> hour, at <NUM>. The sodium sulfate pre-loaded yarn (prepared as described above) was dipped into the gelatin solution with slight stirring for <NUM> minute. The soaked yarn was then taken out from the gelatin solution. After removing excess liquid, the yarn was dried in an oven at <NUM> overnight, generating a coated yarn. After drying, the weight of the yarn was measured again.

A control sample was also prepared by dipping pre-weighed silk yarn (Dharma Trading Co. , tussah silk, <NUM>-ply light, sport weight) directly into the above gelatin solution without pre-treatment with saturated sodium sulfate solution. An increase of yarn weight by <NUM>% was obtained for the control sample, while an increase of yarn weight by <NUM>% was obtained for samples pre-treated with saturated sodium sulfate solution.

A polyurethane solution (SANCURE™ <NUM> original stock emulsion (<NUM>% solids) was used as received in this study. A pre-weighed silk yarn (Dharma Trading Co. , tussah silk, <NUM>-ply light, sport weight) was dipped into the polyurethane solution with slight stirring for <NUM> minutes. The soaked yarn was then taken out from the polyurethane solution and the excess liquid was removed with a doctor blade. The soaked yarn was then directly used for the following gelatin coating process at wet status without any drying treatment.

A gelatin solution was made by dissolving <NUM> of gelatin into <NUM> de-ionized water and stirred at <NUM> rpm for <NUM> hour at <NUM>. The soaked yarn (prepared as described above) at wet status was dipped into the gelatin solution with slight stirring for <NUM> minute. The soaked yarn was then taken out from the gelatin solution. After removing excess liquid, the yarn was dried in an oven at <NUM> overnight, generating a gelatin-coated yarn. After drying, the weight of the yarn was measured again.

A control sample was prepared by dipping pre-weighed silk yarn (Dharma Trading Co. , tussah silk, <NUM>-ply light, sport weight) directly into the above gelatin solution without pre-treatment with polyurethane solution. Another control sample was also prepared by dipping pre-weighed silk yarn directly into polyurethane solution without subsequently coating the yarn with the gelatin solution.

An increase of yarn weight by <NUM>% was obtained for the gelatin-coated control sample without pre-treatment with the polyurethane solution. An increase of yarn weight by <NUM>% was obtained for the control sample coated with only the polyurethane solution. An increase of yarn weight by <NUM>% was obtained after combined treatment of the polyurethane solution and gelatin solution.

A diluted polyurethane solution was prepared by mixing <NUM> SANCURE™ <NUM> original stock emulsion with <NUM> de-ionized water. A pre-weighed silk yarn (Dharma Trading Co. , tussah silk, <NUM>-ply light, sport weight) was dipped into the diluted polyurethane solution with slight stirring for <NUM> minutes. The soaked yarn was then taken out from the diluted polyurethane solution and excess liquid was removed. The soaked yarn was then directly used for the following coating process at wet status without any drying treatment.

A collagen dispersion was made by dispersing <NUM> of Type I bovine collagen into a mixture of <NUM> glacial acetic acid with <NUM> de-ionized water and stirred at <NUM> rpm for <NUM> hours at <NUM>. The soaked yarn (prepared as described above) at wet status was dipped into the collagen dispersion with slight stirring for <NUM> minute. The soaked yarn was then taken out from the collagen dispersion. After removing excess liquid, the yarn was dried in an oven at <NUM> overnight. After drying, the weight of the yarn was measured again.

A control sample was prepared by dipping a pre-weighed silk yarn (Dharma Trading Co. , tussah silk, <NUM>-ply light, sport weight) directly into the above collagen dispersion without the diluted polyurethane solution pretreatment. Another control sample was also prepared by dipping a pre-weighed silk yarn into the diluted polyurethane solution and then dipping the silk yarn into a mixture of <NUM> glacial acetic acid with <NUM> de-ionized water that did not contain collagen.

An increase of yarn weight by <NUM>% was obtained for the collagen dispersion-coated control sample without the diluted polyurethane solution pretreatment. An increase of yarn weight by <NUM>% was obtained for the control sample with only the diluted polyurethane solution pretreatment. An increase of yarn weight by <NUM>% was obtained after the combined treatments of the diluted polyurethane solution pretreatment and collagen dispersion.

A model-<NUM> coaxial spinneret, with an inside needle having an inner diameter of <NUM> inches and an outside needle having an inner diameter of <NUM> inches with a Luer-Lock connecter was purchased from Ramé-Hart Instrument Co. A <NUM>/<NUM> TENCEL™ yarn purchased from Valley Fibers Corporation was pulled through the inside needle of the coaxial spinneret, from the Luer-Lock connector end to the needle tip end, at a constant speed of <NUM>/s (centimeters per second).

A collagen coating solution was prepared by dispersing <NUM> of Type I bovine collagen into <NUM> de-ionized water and stirred at <NUM> rpm for <NUM> hours at <NUM>. Plasticizer (glycerol (<NUM>)) was added into the collagen solution. Additionally, a crosslinker (polyethylene glycol) diglycidyl ether (<NUM>)) was also added into the collagen solution. A NE-<NUM> JUST INFUSION™ syringe pump was used to pump the above collagen solution out of a Becton Dickinson (BD) <NUM> syringe with a Luer-Lock tip, through an inner diameter <NUM> inch polytetrafluoroethylene (PTFE) tube, into the outside needle of the coaxial spinneret by the Luer-Lock connector.

After the yarn exited the coaxial spinneret's needle tip, an array of air driers was used to evaporate the residual water content in the coated materials on the yarn. A rotating yarn winder was used to pull and wind up the coated yarn.

Two model -<NUM> coaxial spinnerets, both with an inside needle having an inner diameter of <NUM> inches and outside needle having an inner diameter of <NUM> inches with a Luer-Lock connector, were purchased from Ramé-Hart Instrument Co. A <NUM>/<NUM> TENCEL™ yarn purchased from Valley Fibers Corporation was pulled through the inside needle of the first coaxial spinneret, from the Luer-Lock connector end to the needle tip end, and entered the inside needle of the second coaxial spinneret, from the Luer-Lock connector end to the needle tip end, at a constant speed of <NUM>/s.

A diluted polyurethane solution was prepared by mixing <NUM> of SANCURE™ <NUM> original stock emulsion with <NUM> de-ionized water. A NE-<NUM> JUST INFUSION™ syringe pump was used to pump the diluted polyurethane solution from a <NUM> BD syringe with a Luer-Lock tip, though a PTFE (polytetrafluoroethylene) tube with an inner diameter of <NUM> inches, into the outside needle of the first coaxial spinneret by the Luer-Lock connector.

A collagen coating solution was prepared by dispersing <NUM> of Type I bovine collagen into <NUM> de-ionized water and stirred at <NUM> rpm for <NUM> hours at <NUM>. Plasticizer (glycerol (<NUM>)) was added into the collagen solution. Additionally, a crosslinker (polyethylene glycol) diglycidyl ether (<NUM>)) was also added into the collagen solution. A NE-<NUM> JUST INFUSION™ syringe pump was used to pump the collagen solution out of a <NUM> BD syringe with a Luer-Lock tip, though a PTFE tube with an inner diameter of <NUM> inches, into the outside needle of the second coaxial spinneret by the Luer-Lock connector.

After the yarn exited the second coaxial spinneret's needle tip, an array of air driers was used to evaporate the residual water content in the coated materials on yarn. A rotating yarn winder was used to pull and wind up the coated yarn.

The coated yarns of Example <NUM> or Example <NUM> are woven on a floor hand loom to create a woven textile.

The coated yarns of Example <NUM> are used as the warp yarns on a dobby loom. The coated yarns of Example <NUM> are used as the weft yarns on the dobby loom to weave a textile.

The coated yarns of Example <NUM> are used as the warp yarns on an industrial jacquard loom. Wool yarns are used as the weft yarns to weave a textile.

The coated yarns of Example <NUM> or Example <NUM> are used for weft knitting with a domestic single bed industrial knitting machine.

The coated yarns of Example <NUM> or Example <NUM> are used for wrap knitting with a domestic double bed industrial knitting machine.

The coated yarns of Example <NUM>, <NUM> and <NUM> are used to make a knit fabric through knit-weaving, jacquard or other knitted structure techniques.

A saturated sodium sulfate solution was prepared by dissolving <NUM> of anhydrous sodium sulfate into <NUM> de-ionized water and stirred at <NUM> rpm for <NUM> hour at room temperature. The precipitation from extra sodium sulfate in the solution was removed by centrifuge. A pre-weighed cotton woven fabric (Whaley's, cotton scrim) was dipped into the saturated sodium sulfate solution with slight stirring for <NUM> minutes. The soaked fabric was then taken out from the salt solution. After removing excess liquid, the fabric was dried in an oven at <NUM> for <NUM> hours, until completely dry, generating a sodium sulfate pre-loaded fabric.

A gelatin solution was made by dissolving <NUM> of gelatin (animal extract, Sigma Aldrich) into <NUM> de-ionized water and stirred at <NUM> rpm for <NUM> hour at <NUM>. The sodium sulfate pre-loaded fabric was dipped into the gelatin solution with slight stirring for <NUM> minute. The fabric was then taken out from the gelatin solution. After removing excess liquid, the fabric was dried in an oven at <NUM> overnight generating a coated fabric. After drying, the weight of the coated fabric was measured again.

A control sample was also prepared by dipping a pre-weighed cotton woven fabric (Whaley's, cotton scrim) directly into the gelatin solution without pre-treatment in the saturated sodium sulfate solution. An increase in fabric weight of <NUM>% was obtained for the control sample, while an increase in fabric weight of <NUM>% was obtained for samples pre-treated with the saturated sodium sulfate solution.

A diluted polyurethane solution was prepared by mixing <NUM> SANCURE™ <NUM> original stock emulsion with <NUM> de-ionized water. A pre-weighed polyester nonwoven fabric (Needlepunched, <NUM> thickness, The Felt Company) was dipped into the diluted polyurethane solution with slight stirring for <NUM> minutes. The soaked fabric was then taken out from the diluted polyurethane solution and excess liquid was removed. The treated fabric was dried in an oven at <NUM> for <NUM> hours, until completely dry, generating a polyurethane pre-loaded fabric.

A gelatin solution was made by dissolving <NUM> of gelatin (animal extract, Sigma Aldrich) into <NUM> de-ionized water and stirred at <NUM> rpm for <NUM> hour at <NUM>. The polyurethane pre-load fabric was dipped into the gelatin solution with slight stirring for <NUM> minute. The fabric was then taken out from the gelatin solution. After removing excess liquid, the fabric was dried in an oven at <NUM> overnight, generating a coated fabric. After drying, the weight of the coated fabric was measured again.

A control sample was prepared by dipping a pre-weighed polyester nonwoven fabric (Needlepunched, <NUM> thickness, The Felt Company) directly into the gelatin solution without pretreatment in the diluted polyurethane solution. An increase in fabric weight of <NUM>% was obtained for the control sample, while an increase in fabric weight of <NUM>% was obtained for samples pre-treated with the diluted polyurethane solution.

A collagen solution was made by dissolving <NUM> of Type I bovine collagen in <NUM> de-ionized water with <NUM> N HCl (hydrochloric acid) at room temperature with vigorous stirring for <NUM> hours. After a homogenous collagen solution was formed, <NUM> of 10x PBS (phosphate-buffered saline) stock solution was added, and the solution's pH was adjusted to <NUM> by adding sodium hydroxide. The solution was stirred at <NUM> for six hours.

A silk yarn was dipped into the coating solution prepared above for at least <NUM> seconds. After removing excess liquid, the collagen solution-soaked yarn was then transferred in pure CARBITOL (di(ethylene glycol) ethyl ether) for coagulation for at least <NUM> seconds. The CARBITOL coagulated yarn was then transferred into acetone for at least <NUM> seconds to remove CARBITOL. The processed yarn was then dried at room temperature with high flow speed air. The collagen uptake, compared to original non-coated yarns, was about <NUM>% to about <NUM>%, in weight percent.

A collagen solution was made by dispersing <NUM> of Type I bovine collagen in <NUM> <NUM> N hydrochloric acid and stirred at <NUM> rpm for <NUM> hours at <NUM>. The collagen was then cooled to <NUM>, and <NUM> of 10X phosphate buffer saline, which was adjusted to pH <NUM> using <NUM> N sodium hydroxide, was added to the cold mixture, resulting in a collagen solution at conditions for fibrillation, pH <NUM>-<NUM> and conductivity of <NUM>-<NUM>/cm. A pre-weighed silk yarn was dipped into the cold collagen solution with slight stirring for <NUM> minutes. The soaked yarn was then taken out from the cold collagen solution and excess liquid was removed. The soaked yarn was then placed directly into a <NUM> bath of diethylene glycol monobutyl ether (CARBITOL) with slight stirring for <NUM> minute. The yarn was then dried in a <NUM> oven for four hours. The collagen uptake, compared to original non-coated yarns, was about <NUM>% to about <NUM>%, in weight percent.

While various embodiments have been described herein, they have been presented by way of example, and not limitation. It should be apparent that adaptations and modifications are intended to be within the meaning and range of equivalents of the disclosed embodiments, based on the teaching and guidance presented herein. It therefore will be apparent to one skilled in the art that various changes in form and detail can be made to the embodiments disclosed herein without departing from the spirit and scope of the present disclosure. The elements of the embodiments presented herein are not necessarily mutually exclusive, but can be interchanged to meet various situations as would be appreciated by one of skill in the art.

Embodiments of the present disclosure are described in detail herein with reference to embodiments thereof as illustrated in the accompanying drawings, in which like reference numerals are used to indicate identical or functionally similar elements. References to "one embodiment," "an embodiment," "some embodiments," "in certain embodiments," etc., indicate that the embodiment described can include a particular feature, structure, or characteristic, but every embodiment can not necessarily include the particular feature, structure, or characteristic.

The examples are illustrative, but not limiting, of the present disclosure.

Claim 1:
A protein-coated material comprising:
a substrate, wherein the substrate is selected from the group consisting of a textile, a sheet, a rope, a fiber, a yarn, a strand, and combinations thereof;
a salt coating disposed over the substrate, wherein the salt is sodium sulfate; and
a protein coating disposed over the salt coating, wherein the protein is gelatin.