Source: https://www.federalregister.gov/documents/2005/05/20/05-10064/government-owned-inventions-availability-for-licensing
Timestamp: 2018-09-25 09:27:34
Document Index: 673809869

Matched Legal Cases: ['Application No. 60', 'Application No. 60', 'Application No. 60', 'Application No. 60', 'Application No. 60', 'Application No. 60', 'Application No. 10', 'Application No. 037183431']

70 FR 29332
29332-29334 (3 pages)
Methods and Compositions for the ex vivo High-Throughput Detection of Protein/Protein Interactions
Lepirudin Adsorbed to Catheter
VAC-BAC Shuttle Vector System
https://www.federalregister.gov/d/05-10064 https://www.federalregister.gov/d/05-10064
Louis J. Rezanka (NIA), U.S. Provisional Application No. 60/623,762 filed 29 Oct 2004 (DHHS Reference No. E-330-2004/0-US-01)
Available for licensing and commercial development is a method of synthesizing EPC (4-Nitrophenyl-6-(O-phosphocholine) hydroxyhexanoate) and methods of synthesizing phosphocholine analogues and the phosphocholine conjugates formed therefrom. These molecules have clinical and research applications as anti-microbial agents. Specifically, EPC conjugated to protein carriers has been demonstrated to generate a protective immune response to Streptococcus pneumoniae. The invention provides a process for EPC synthesis as well as for its reaction intermediates for use in synthesis.
In addition to licensing, the technology is available for further development through collaborative research opportunities with the inventors. Start Printed Page 29333
Sankar Adhya and Amos Oppenheim (NCI), U.S. Provisional Application No. 60/629,933 filed 23 Nov 2004 (DHHS Reference No. E-264-2004/0-US-01)
This invention relates to methods and compositions for the high-throughput detection of protein-protein interactions using a lambda phage display system. One of the central challenges in systems biology is defining the interactome, or set of all protein-protein interactions within a living cell, as a basis for understanding biological processes for early diagnosis of disease and for drug development. The invention provides a novel proteomic toolbox for high-throughput medical research based in combining phage lambda protein display and recent advances in manipulation of the phage's genome. The method uses the bacteriophage lambda vector to express proteins on its surface, and is based on the use of mutant phage vectors such that only interacting phages will be able to reproduce and co-infect an otherwise non-permissive host and produce plaques. The invention allows for the characterization of bacteriophage display libraries that could be easily adapted to be used in large-scale functional protein chip assays.
Phillip Heller (NIA), U.S. Provisional Application No. 60/602,651 filed 19 Aug 2004 (DHHS Reference No. E-116-2004/0-US-01)
Licensing Contact: Susan O. Ano; (301) 435-5515; anos@mail.nih.gov.
The described technology is a biodegradable microbead or microparticle, useful for the sustained localized delivery of biologically active proteins or other molecules of pharmaceutical interest. The microbeads are produced from several USP grade materials, a cationic polymer, an anionic polymer and a binding component (e.g., gelatin, chondroitin sulfate and avidin), in predetermined ratios.) Biologically active proteins are incorporated into preformed microbeads via an introduced binding moiety under nondenaturing conditions.
Proteins or other biologically active molecules are easily denatured, and once introduced into the body, rapidly cleared. These problems are circumvented by first incorporating the protein into the microbead. Microbeads with protein payloads are then introduced into the tissue of interest, where the microbeads remain while degrading into biologically innocuous materials while delivering the protein/drug payload for adjustable periods of time ranging from hours to weeks. This technology is an improvement of the microbead technology described in U.S. Patent No. 5,759,582.
This technology has two commercial applications. The first is a pharmaceutical drug delivery application. The bead allows the incorporated protein or drug to be delivered locally at high concentration, ensuring that therapeutic levels are reached at the target site while reducing side effects by keeping systemic concentration low. The microbead accomplishes this while protecting the biologically active protein from harsh conditions traditionally encountered during microbead formation/drug formulation.
Second, the microbeads and microparticles can be used in various research assays, such as isolation and separation assays, to bind target proteins from biological samples. A disadvantage of the conventional methods is that the proteins become denatured. The denaturation results in incorrect binding studies or inappropriate binding complexes being formed. The instant technology corrects this disadvantage by using a bead created in a more neutral pH environment. It is this same environment that is used for the binding of the protein of interest as well.
McDonald Horne (CC), U.S. Provisional Application No. 60/436,439 filed 23 Dec 2002 (DHHS Reference No. E-295-2002/0-US-01); PCT Application No. PCT/US03/40888 filed 22 Dec 2003, which published as WO 2004/058324 A2 on 15 Jul 2004 (DHHS Reference No. E-295-2002/0-PCT-02)
Licensing Contact: Michael Shmilovich; (301) 435-5018; shmilovm@mail.nih.gov.
The invention is a method for preventing venous access device (VAD) thrombosis by coating the VAD catheter with lepirudin, which has been found to be readily adsorbed by the silicone rubber of the VADs, and is expected to have good retention properties. VADs typically remain in place for weeks or months and sometimes cause clotting (thrombosis) of the veins. Accordingly, the simple technique of soaking a silicone catheter in lepirudin before venous insertion is the gist of the invention. Chronically ill patients who must be catheterized for long periods of time will benefit particularly from this technique which promises to reduce swelling and pain associated with VAD-induced thrombosis.
Reference: Horne, MK, Brokaw, KJ. Antithrombin activity of lepirudin adsorbed to silicone (polydimethylsiloxane) tubing. Thrombosis Research 2003; 112:111-115.
Bernard Moss, Arban Domi (NIAID), U.S. Provisional Application No. 60/371,840 filed 10 Apr 2002 (DHHS Reference No. E-355-2001/0-US-01); U.S. Provisional Application No. 60/402,824 filed 09 Aug 2002 (DHHS Reference No. E-355-2001/1-US-01); International Patent Application No. PCT/US03/11183 filed 10 Apr 2003, which published as WO 03/087330 A2 on 23 Oct 2003 (DHHS Reference No. E-355-2001/2-PCT-01); U.S. Patent Application No. 10/959,392 filed 05 Oct 2004 (DHHS Reference No. E-355-2001/2-US-02); European Patent Application No. 037183431 filed 10 Apr 2003 (DHHS Reference No. E-355-2001/2-EP-03)
Licensing Contact: Robert M. Joynes; (301) 594-6565; joynesr@mail.nih.gov.
The following are some of the uses for a VAC-BAC:
1. VAC-BACs can be used to modify vaccinia virus DNA by deletion, insertion or point mutation or add new DNA to the VAC genome with methods developed for bacterial plasmids, rather Start Printed Page 29334than by recombination in mammalian cells.
2. It can be used to produce recombinant vaccinia viruses for gene expression.
3. It can be used for the production of modified vaccinia viruses that have improved safety or immunogenicity.
Advantages of the VAC-BAC shuttle system:
1. VAC-BACs are clonally purified from bacterial colonies before virus reconstitution in mammalian cells.
2. Manipulation of DNA is much simpler and faster in bacteria than in mammalian cells.
3. Modified genomes can be characterized prior to virus reconstitution.
4. Only virus with modified genomes will be produced so that virus plaque isolations are not needed.
5. Generation of a stock of virus from a VAC-BAC is accomplished within a week rather than many weeks.
6. Multiple viruses can be generated at the same time since plaque purification is unnecessary.
1. Domi, A., and B. Moss. 2002. Cloning the vaccinia virus genome as a bacterial artificial chromosome in Escherichia coli and recovery of infectious virus in mammalian cells. Proc. Natl. Acad. Sci. USA 99:12415-12420.
2. Domi, A., and B. Moss. 2005. Engineering of a vaccinia virus bacterial artificial chromosome in Escherichia coli by bacteriophage lambda-based recombination. Nature Methods 2:95-97.
[FR Doc. 05-10064 Filed 5-19-05; 8:45 am]