Interleukin 1β protease and interleukin 1β...

Details Interleukin 1β protease and interleukin 1β... Interleukin 1β protease and interleukin 1β...

2006-02-07

2006-02-07

Henley, III, Raymond (Department: 1614)

Drug, bio-affecting and body treating compositions

Designated organic active ingredient containing

Peptide containing doai

C514S017400, C514S019300

Reexamination Certificate

active

06995141

ABSTRACT:
There is disclosed an isolated polypeptide and derivatives thereof having protease biological activity for human precursor IL-1β and for a substrate comprising:in-line-formulae description="In-line Formulae" end="lead"?R1—Asp—R2—R3in-line-formulae description="In-line Formulae" end="tail"?wherein R1and R3are independently any D or L isomer amino acid, R2is Ala or Gly, and wherein the specific protease cleavage site is between Asp and R2. Inhibitor compounds, compositions and methods for inhibiting Interleukin 1β protease activity are also disclosed. The inhibitor compounds comprise an amino acid sequence of from 1 to about 5 amino acids having an N-terminal blocking group and a C-terminal Asp residue connected to an electronegative leaving group, wherein the amino acid sequence corresponds to the sequence Ala-Tyr-Val-His-Asp.

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CAPLUS DN 116 50949, Rosenthal et al.J. Clin. Invest.88, 1467 (Abstract) (1991).
CAPLUS DN 118: 208112, Thornberry et al.Nature35, 768 (Abstract) (1992).
Casano et al. The structure and complete nucleotide sequence of the murine gene encoding interleukin-1β converting enzyme (ICE).Genomics20, 474 (1994).
Cerretti et al. Molecular cloning of the IL-1β processing enzyme.J. Cell. Biol.Supp. F15, P506 (1991).
Cerretti et al. Molecular cloning of the IL-1β processing enzyme.Cytokinep. 137 (1991).
Cheremisinoff et al. (eds).Biotechnology Applications and Research, Technomics Publishing Co, Inc. pp. 21, 541-557 (1985).
Dower et al. The interleukin-1 system: Receptors, ligands and signals.Chem. Immunol.51, 33 (1992).
Dreyer et al. Inhibition of human Immunodeficiency virus 1 protease in vitro: rational design of substrate analogue inhibitors.Proc. Natl. Acad. Sci. USA86, 9752 (1989).
Hazuda et al. The kinetics of interleukin 1 secretion from activated monocytes.J. Biol. Chem.263, 8473 (1988).
Howard et al. IL-1-converting enzyme requires aspartic acid residues for processing of the IL-1β precursor at two distinct sites and does not cleave 31-κDa IL-1a.J. Immunol.147, 2964 (1991).
Kitada et al. New peptide models for studying racemization.Chem. Pharm. Bull.26, 585 (1978).
Knittel et al. Stimulation of insulin secretion from pancreatic Islets by the cholecystokinin-tetrapeptide analogs Trp-Pro-Asp-Phe-NH2and Trp-Pro-Asp-Phe(4′-NO2)-NH2.Pept. Res.3, 224 (1990).
Koga et al. Comparative study on specifics of rat cathepsin L and papain: amino acid differences as substrate binding sites are involved in their specificities.J. Biochem.108, 976 (1990).
Kostura et al. Identification of a monocyte specific pre-interleukin 1β convertase activity.Proc. Natl. Acad. Sci USA86, 5227 (1989).
Lee et al. Generation of cDNA probes directed by

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