Drug – bio-affecting and body treating compositions – Designated organic active ingredient containing – Peptide containing doai
Reexamination Certificate
2006-09-12
2006-09-12
Campell, Bruce R. (Department: 1654)
Drug, bio-affecting and body treating compositions
Designated organic active ingredient containing
Peptide containing doai
C514S002600, C514S019300
Reexamination Certificate
active
07105483
ABSTRACT:
The invention relates to the use of phosphinic pseudopeptide derivatives for production of a medicament for selectively inhibiting the active C-terminal site of angiotensin I converting enzyme. These derivatives are of formula (II):where, R1may be a protecting group for amino functions usually used in peptide chemistry or an amino acid or a peptide protected by the above type of protecting groups, R2and R3correspond to a natural or unnatural amino acid side chain and R4and R5represent a hydrogen atom or a counterion.
REFERENCES:
patent: 5476847 (1995-12-01), McKittrick et al.
patent: 5500414 (1996-03-01), Dive et al.
patent: 5776903 (1998-07-01), Dive et al.
patent: 6482797 (2002-11-01), Dive et al.
patent: 0 361 341 (1990-04-01), None
patent: 361341 (1990-04-01), None
patent: 0 725 075 (1996-08-01), None
patent: 2 676 059 (1992-11-01), None
patent: 2 781 230 (2000-01-01), None
patent: WO 200001706 (2000-01-01), None
Demange, L. et al. “Synthesis of phosphinic alanyl-proline surrogates Ala psi (P02R-CH) Pro as potential inhibitors of the human cyclophilin hCyp-18”, Tetrahedron Letters, Elsevier Science Publishers, Amsterdam, NL, vol. 42, no. 36, pp. 6295-6297, XP004302932, ISSN: 0040-4039, Sep. 3, 2001.
Dzau, Victor J. “Tissue Angiotensin and Pathobiology of Vascular Disease: A Unifying Hypothesis”, Hypertension. vol. 37, pp. 1047-1052 2001.
Linz, Wolfgang et al. “Contribution of Kinins to the Cardiovascular Actions of Angiotensin-Converting Enzyme Inhibitors” Pharmacological Reviews. vol. 47, no. 1, pp. 25-49 1995.
Soubrier, Florent et al, “Two putative active centers in human angiotensin I-converting enzyme revealed by molecular cloning”, Biochemistry, vol. 85 pp. 9386-9390 1998.
Wei, Lei et al. “The Two Homologous Domains of Human Angiotensin I-converting Enzyme are Both Catalytically Active”, The Journal of Biological Chemistry, vol. 266, No. 14, pp. 9002-9008, 1991.
Jaspard, Emmanuel et al. “Differences in the Properties and Enzymatic Specificities of the Two Active Sites of Angiotensin I-converting Enzyme (Kininase II)”, The Journal of Biological Chemistry, vol. 268, No. 13, pp. 9496-9503 1993.
Azizi, Michel et al. “Acute Angiotensin-converting Enzyme Inhibition Increases the Plasma Level of the Natural Stem Cell Regulator N-Acetyl-Seryl-Aspartyl-Lysyl-Proline”, J. Clin. Invest., vol. 97, No. 3, pp. 839-844 1996.
Dive, Vincent et al. “RXP 407, a phosphinic peptide, is a potent inhibitor of angiotensin I converting enzyme able to differentiate between its two active sites”, Biochemistry, vol. 96, pp. 4330-4335 1999.
Junot, Christophe et al. “RXP 407, a Selective inhibitor of the N-Domain of Angiotensin I-Converting Enzyme, Blocks in Vivo the Degradation of Hemoregulatory Peptide Acetyl-Ser-Asp-Lys-Pro with No Effect on Angiotensin I Hydrolysis”, The Journal of Pharmacology and Experimental Therapeutics, vol. 297, No. 2, pp. 606-611 2001.
Jiracek, Jiri et al. “Development of Highly Potent and Selective Phosphinic Peptide Inhibitors of Zinc Endopeptidase 24-15 Using Combinatorial Chemistry”, The Journal of Biological Chemistry, vol. 270, No. 37, pp. 21701-21706 1995.
Jiracek, Jiri et al. “Development of the First Potent and Selective Inhibitor of the Zinc Endopeptidase Neurolysin Using a Systematic Approach Based on Combinatorial Chemistry of Phosphinic Peptides”, The Journal of Biological Chemistry, vol. 271, No. 32, pp. 19606-19611 1996.
Yiotakis, Athanasios et al. “Protection of the Hydroxyphosphinyl Function of Phosphinic Dipeptides by Adamantyl. Application to the Solid-Phase Synthesis of Phosphinic Peptides”, The Journal of Organic Chemistry, vol. 61, No. 19, pp. 6601-6605 1996.
Vassiliou, Stamatia et al. “Phosphinic Pseudo-Tripeptides as Potent Inhibitors of Matrix Metalloproteinases: A Structure-Activity Study”, Journal of Medicinal Chemistry, vol. 42, No. 14, pp. 2610-2620 1999.
Georgiadis, Dimitris et al. “Potent and Selective Inhibition of Zinc Aminopeptidase A (EC 3.4.11.7, APA) by Glutamyl Aminophosphinic Peptides: Importance of Glutamyl Aminophosphinic Residue in the P1 Position”, Biochemistry, vol. 39, No. 5, pp. 1152-1155 2000.
Greene, Theodora W. et al. “The Role of Protective Groups in Organic Synthesis” and “Protection for the Amino Group”, Protective Groups in Organic Synthesis, 2nded., pp. 1, 309-315 1991.
Baylis, E. et al. “1-Aminoalkylphosphonous Acids. Part 1. Isosteres of the Protein Amino Acids”, J. Chem.Soc. Perkin Trans., pp. 2845-2853 1984.
Villieras, J. et al. “The Wittig-Homer Reaction in Heterogenous Media VIII. Cyclisation During the Aldolisation Step from Aqueous Glutaraldehyde”, pp. 149-157 1986.
Chen, Huixiong et al. “Long Lasting Antinociceptive Properties of Enkephalin Degrading Enzyme (NEP and APN) Inhibitor Prodrugs”, J. Med. Chem., vol. 44, pp. 3523-3530 2001.
Cotton Joel
Dive Vincent
Georgiadis Dimitri
Campell Bruce R.
Commissariat a l''Energie Atomique
Kosar Andrew D.
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