Chemistry: molecular biology and microbiology – Measuring or testing process involving enzymes or... – Involving antigen-antibody binding – specific binding protein...
Reexamination Certificate
2008-07-01
2008-07-01
Campell, Bruce R. (Department: 1648)
Chemistry: molecular biology and microbiology
Measuring or testing process involving enzymes or...
Involving antigen-antibody binding, specific binding protein...
C424S204100
Reexamination Certificate
active
07393658
ABSTRACT:
Prion protein binding materials and methods for using the binding materials to detect or remove a prion protein from a sample, such as a biological fluid or an environmental sample. The binding materials are capable of binding to one or more forms of prion protein including cellular prion protein (PrPc), infectious prion protein (PrPsc), recombinant prion protein (PrPr), and proteinase resistant prion protein (PrPres). Prions from various species, including humans and hamsters, are bound by the binding materials.
REFERENCES:
patent: 5010175 (1991-04-01), Rutter et al.
patent: 5133866 (1992-07-01), Kauvar
patent: 5281539 (1994-01-01), Schramm
patent: 5312730 (1994-05-01), Piran et al.
patent: 5498538 (1996-03-01), Kay et al.
patent: 5750361 (1998-05-01), Prusiner et al.
patent: 5808011 (1998-09-01), Gawryl et al.
patent: 5834318 (1998-11-01), Buettner et al.
patent: 5888834 (1999-03-01), Ishikawa et al.
patent: 6221614 (2001-04-01), Prusiner et al.
patent: 6379905 (2002-04-01), Fishleigh et al.
patent: 6437102 (2002-08-01), Lee et al.
patent: 6451541 (2002-09-01), Winnacker et al.
patent: 6750025 (2004-06-01), Hammond et al.
patent: 2003/0092094 (2003-05-01), Vey et al.
patent: WO 92/00091 (1992-01-01), None
patent: WO 01/77687 (2001-10-01), None
patent: WO 03/016904 (2003-02-01), None
Foster et a., Studies on the removal of abnormal prion protein by Processes used in the manufacture of human plasma products. (2000) Vox sanginis. vol. 78, p. 86-95.
Kragtenet al., Glyceraldehyde-3-phosphate Dehydrohenase, the Putative Target of Antiapoptotic Compounds CGP 3466 and R-(-)-Deprenyl. (1998) Journal of Biological Chemistry vol. 273, No. 10. p. 5821-5828.
Tosoh Bioscience LLc, Data Sheet and Manual, www.tosohbioscience.com.
Aubry et al., “N-Methyl Peptides. IV. Water and Beta-Turn in Peptides. Crystal Structure of N-Pivaloyl-L-Prolyl-N, N′-Dimethyl-D-Alaninamide in the Anhydrous and Monohydrated States”,Int. J. Pept. Protein Res., 18: 195-202 (1981).
Caughey, B., et al., “Binding of the Protease-Sensitive Form of Prion Protein PrP to Sulfated Glycosaminoglycan and Congo Red”,Journal of Virology, 68: 2135-2141 (1994).
Degrado, W.F., “Design of Peptides and Proteins”,Adv. Protein Chem:.39, 51-124, (1988).
Devlin, J.J. et al., “Random Peptide Libraries: A Source of Specific Protein Binding Molecules”,Science: 249, 404-406 (1990).
Fischer, M.B. et al., “Binding of Disease-Associated Prion Protein to Plasminogen”,Nature: 408, 479-483 (2000).
Furka, A. et al. “General Method for Rapid Synthesis of Multicomponent Peptide Mixtures”,Int. J. Peptide Protein Res.:37, 487-493 (1991).
Ingrosso, L., et al., “Congo Red Prolongs the Incubation Period in Scrapie-Infected Hamsters”,Journal of Virology: 69, 506-508 (1995).
Jameson, B.A. et al., “A Rationally Designed CD4 Analogue Inhibits Experimental Allergic Encephalomyelitis”,Nature: 368, 744-746 (1994).
Kascsak, R.J., et al., “Immunodiagnosis of Prion Disease”,Immunological Invest.: 26, 259-268 (1997).
Lam, K.S. et al., “A New Type of Synthetic Peptide Library for Identifying Ligand-Binding Activity”,Nature: 354,82-84 (1991).
Soto et al., “Reversion Of Prion Protein Conformational Changes By Synthetic β-Sheet Breaker Peptides”,Lancet: 355, 192-197 (2000).
Merrifield, B. “Solid Phase Synthesis”,Science: 232, 341-3479 (1986).
Needleman, S.B. et al. “A General method Applicable to the Search for Similarities in the Amino Acid Sequence of Two Proteins”,J. Mol. Biol.: 48, 443-453 (1970).
Pearson, W.R. et al. “Impoved Tools for Biological Sequence Comparison”,Proc. Natl. Acad. Sci. U.S.A.:85, 2444-2448 (1988).
Priola, S.A., et al., “Porphyrin and Phthalocyanine Antiscrapie Compounds”,Science: 287, 1503-1506 (2000).
Prusiner, S.B., “Molecular Biology of Prion Diseases”,Science: 252, 1515-1522 (1991).
Rose et al. “Turns In Peptides And Proteins”,Molecular Biology of Prion Diseases Adv. Protein Chem.: 37, 1-109 (1985).
Safar, J. et al., “Eight Prion Strains Have PrP(Sc) Molecules With Different Conformations”,Nature Medicine: 4, 1157-1165 (1998).
Samson, W.K. et al. “A 35 Amino Acid Fragment of Leptin Inhibits Feeding in the Rat”,Endocrinology: 137, 5182-5185 (1996).
Soto, C. et al., “Reversion of Prion Protein Conformational Changes in Synthetic Beta-Sheet Breaker Peptides”,Lancet: 355, 192-197 ( 2000).
Stockell, et al., “Prion Protein Selectively Bindes Copper(II) Ions”,Biochemistry: 37, 7185-7193 (1998).
Tagliavani, F., et al., “Effectiveness of Anthracycline Against Experimental Prion Diseases in Syrian Hamsters,”Science: 276, 1119-1122 (1997).
Caspi et al., “The Anti-Prion Activity Of Congo Red”, J. Biol. Chem.: 273, 3484-3489 (1999).
McHattle et al., “Clusterin Prevents Aggregation Of Neuropeptide 106-126 In Vitro”,Biochem. Biophys. Res. Commun: 259, 336-340 (1999).
Burton Steven J.
Carbonell Ruben G.
Gurgel Patrick V.
Hammond David J.
Shen Honglue
Boesen Agnieszka
Campell Bruce R.
Nixon & Peabody LLP
North Carolina State University
Pathogen Removal and Diagnostic Technologies, Inc.
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