Transframe peptide inhibitor of viral protease

Chemistry: natural resins or derivatives; peptides or proteins; – Peptides of 3 to 100 amino acid residues – 11 to 14 amino acid residues in defined sequence

Patent

Rate now

  [ 0.00 ] – not rated yet Voters 0   Comments 0

Details

530328, 530329, 530330, 4241601, 4242081, 536 231, 536 2353, A61K 3804, A61K 3942, C07K 500, C07H 2102

Patent

active

058722106

ABSTRACT:
The present invention describes small, water soluble peptides isolated from a native virus inhibitory sequence that blocks maturation of the virally encoded protease and inhibits the mature protease as well. The peptides may be used in the treatment of virally infected cells, in the preparation of vaccine formulations, in the generation of clinically relevant antibodies and anti-idiotypic antibodies and in the generation of a screening assay or kit that can be used to identify other similarly acting protease inhibitors.

REFERENCES:
patent: 5087557 (1992-02-01), McClure
patent: 5188950 (1993-02-01), Balani et al.
patent: 5245015 (1993-09-01), Fung et al.
patent: 5342922 (1994-08-01), Marshall et al.
Szewczuk, A., et al., "Specificity of .gamma.-Glutamyl Cyclotransferase", Can. J. Biochem., 53:706-712 (1975).
Szewczuk, A., et al., "Specificity of .gamma.-Glutamyl Cyclotransferase", Chemical Abstracts, vol. 83, abstract No. 92952 (1975).
Yamamoto, Y., et al., "Synthesis of Hexatriacontapeptide Amide Corresponding to the Proposed Structure of Neuropeptide Y (NPY)", Peptide Chemistry, 317-322 (1985).
Yamamoto, Y., et al. "Synthesis of Hexatriacontapeptide Amide Corresponding to the Proposed Structure of Neuropeptide Y (NPY)", Chemical Abstracts, vol. 103, abstract No. 123894 (1985).
Cason, J., et al. "Identification of Immunogenic Regions of the Major Coat Protein of Human Papillomavirus Type 16 that Contain Type-restricted Epitopes" J. Gen. Virol., 70:2973-2987 (1989).
Cason, J., et al. "Identification of Immunogenic Regions of the Major Coat Protein of Human Papillomavirus Type 16 that Contain Type-restricted Epitopes", Chemical Abstracts, vol. 112, abstract No. 116820 (1989).
Slootstra, J., et al., "Structural aspects of antibody-antigen interaction revealed through small randam peptide libraries", Molecular Diversity, 1:87-96 (1995).
Slootstra, J., et al., "Structural aspects of antibody-antigen interaction revealed through small randam peptide libraries", Chemical Abstracts, vol. 124, abstract No. 257898.
Robinson, Michael B., et al., "Hydrolysis of the Brain Dipeptide N-Acetyl-L-aspartyl-L-glutamate", The Journal of Biological Chemistry, 262:14498-14506 (1987).
Anderson, D.C., et al. "Exact Definition of Species-Specific and Cross-Reactive Epitopes of the 65-kilodalton Protein of Mycobacterium leprae Using Synthetic Peptides", The Journal of Immunology, 141:607-613 (1988).
Battle, J.K., et al. "Immunological Characterization of the gag Gene Products of Bovine Immunodeficiency Virus," Journal of Virology, 66:6868-6877 (1992).
Zybarth, G., et al., "Domains Upstream of the Protease (PR) in Human Immunodeficiency Virus Type 1 Gag-Pol Influence PR Autoprocessing", Journal of Virology, 69:3878-3884 (1995).
Giam, Chou-Zen, et al. "In Vivo and in Vitro Autoprocessing of Human Immunodeficiency Virus Protease Expressed in Escherichia coli," The Journal Biological Chemistry, 263: 14617-14620 (1988).
Strickler, James E., et al. "Characterization and Autoprocessing of Precursor and Mature Forms of Human Immunodeficiency Virus Type (HIV 1) Protease Purified From Escherichia coli", Proteins: Structure, Function and Genetics, 6:139-154 (1989).
Louis, J. L., et al. "Autoprocessing of the HIV-1 protease using purified wild-type and mutated fusion proteins expressed at high levels in Escherichia coli", Eur. J. Biochem. 199, 361-369 (1991).
Reil, H., et al. "A Heptanucleotide Sequence Mediates Ribosomal Frameshifting in Mammalian Cells", Journal of Virology, 67:5579-5584, (1993).
Zybarth, Gabrielle, et al. "Proteolytic Activity of Novel Human Immunodeficiency Virus Type 1 Proteinase Proteins from a Precursor with a Blocking Mutation at the N Terminus of the PR Domain", Journal of Virology, 68:240-250 (1994).
Louis, John M., et al. "Kinetics and mechanism of autoprocessing of human immunodeficiency virus type 1 protease from an analog of the Gag-Pol polyprotein", Proc. Nat'l Acad. Sci., 9:7970-7974 (1994).
Wondrak, Ewald M., et al. "Removal of Zinc is Required for Processing of the Mature Nucleocapsid Protein of Human Immunodeficiency Virus, Type 1, by the Viral Protease", The Journal of Biological Chemistry, 269: 21948-21950 (1994).
Miller, Michael D., et al. "Advances in Automated Docking Applied to Human Immunodeficiency Virus Type 1 Protease", Methods in Enzymology, 241: 354-70 (1994).
Ringe, D., "X-Ray Structures of Retroviral Proteases and Their Inhibitor-Bound Complexes", Methods in Enzymology, 241:157-177 (1994).
Vacca, J. P., "Design of Tight-Binding Human Immunodeficiency Virus Type 1 Protease Inhibitors", Methods in Enzymology, 241:311-334 (1994).
Kempf, D.J., "Design of Symmetry-Based, Peptidomimetic Inhibitors of Human Immunodeficiency Virus Protease", Methods in Enzymology, 241:334-354 (1994).
Balani, S.K., et al. "Metabolism of L-689,502 by Rat Liver Slices to Potent HIV-1 Protease Inhibitors", Drugs Metabolism and Disposition, 23:185-189 (1995).

LandOfFree

Say what you really think

Search LandOfFree.com for the USA inventors and patents. Rate them and share your experience with other people.

Rating

Transframe peptide inhibitor of viral protease does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Transframe peptide inhibitor of viral protease, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Transframe peptide inhibitor of viral protease will most certainly appreciate the feedback.

Rate now

     

Profile ID: LFUS-PAI-O-2063105

  Search
All data on this website is collected from public sources. Our data reflects the most accurate information available at the time of publication.