Tailoring self-assembly of proteins on solid surfaces remains a great challenge in diverse fields, e.g., enzyme catalysis, biosensing, and biomineralization, where surface functions are retained by controlling molecular structures. As a new approach in designing surface chemistry, we use here biocombinatorially selected graphite binding dodecapeptides which form self-assembled, long-range ordered peptide nanostructures on graphite. The peptide is engineered via simple sequence mutations to control fundamental processes of self-assembly, e.g., binding to solid surfaces, growth kinetics, and intermolecular interactions. Using atomic force microscopy and contact angle studies, we identify three domains of amino acids along the primary sequence that steer peptide aggregation and ordering, leading to uniformly displayed residues and sequence-programmable surface chemistries. Short peptides, with easily designed sequences, offer versatile control over molecular functionalization at liquid-solid interfaces, resulting in well-defined surface properties and nanoscale topology essential in building engineered, chemically rich, bio-solid interfaces.
This paper has been withdrawn by the author due to a missing figure
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Tailoring self-assembly of proteins on solid surfaces remains a great challenge in diverse fields, e.g., enzyme catalysis, biosensing, and biomineralization, where surface functions are retained by controlling molecular structures. As a new approach in designing surface chemistry, we use here biocombinatorially selected graphite binding dodecapeptides which form self-assembled, long-range ordered peptide nanostructures on graphite. The peptide is engineered via simple sequence mutations to control fundamental processes of self-assembly, e.g., binding to solid surfaces, growth kinetics, and intermolecular interactions. Using atomic force microscopy and contact angle studies, we identify three domains of amino acids along the primary sequence that steer peptide aggregation and ordering, leading to uniformly displayed residues and sequence-programmable surface chemistries. Short peptides, with easily designed sequences, offer versatile control over molecular functionalization at liquid-solid interfaces, resulting in well-defined surface properties and nanoscale topology essential in building engineered, chemically rich, bio-solid interfaces.
This paper has been withdrawn by the author due to a missing figure