Drug – bio-affecting and body treating compositions – Designated organic active ingredient containing – Having -c- – wherein x is chalcogen – bonded directly to...
Reexamination Certificate
2011-07-19
2011-07-19
Hui, San-ming (Department: 1628)
Drug, bio-affecting and body treating compositions
Designated organic active ingredient containing
Having -c-, wherein x is chalcogen, bonded directly to...
Reexamination Certificate
active
07981922
ABSTRACT:
This invention relates to a process for synthesizing an amino acid derivative of a tripeptidomimetic, such as lisinopril. The invention also relates to a derivative of lisinopril, incorporating a amino acid moeity such as tryptophan at the P2′ position.
REFERENCES:
patent: 4356118 (1982-10-01), Owens
patent: 4374829 (1983-02-01), Harris et al.
patent: 5008273 (1991-04-01), Schnorrenberg et al.
patent: WO 2004/087743 (2004-10-01), None
Almquist, R. et al., “Derivatives of the potent angiotensin converting enzyme inhibitor 5(S)-benzamido-4-oxo-6-phenylhexanoyl-L-proline: effect of changes at positions 2 and 5 of the hexanoic acid portion,” J. Med. Chem., 1982, 25:1292-1299.
Almquist, R. et al., “Synthesis and biological activity of a ketomethylene analog of a tripeptide inhibitor of angiotensin converting enzyme,” J. Med. Chem., 1980, 23:1392-1398.
Antonios, T. et al., “Angiotensin converting enzyme inhibitors in hypertension: potential problems,” J. Hypertens, 1995, 13(Suppl 3): S11-S16.
Bala, M. et al., “Novel Peptidomimics as Angiotensin-Converting Enzyme Inhibitors: A Combinatorial Approach,” Bioorganic & Medicinal Chemistry, 2002, 10:3685-3691.
Borghi, C. et al., “Double-blind comparison between zofenopril and lisinopril in patients with acute myocardial infarction: Results of the Survival of Myocardial Infarction Long-Term Evaluation-2 (SMILE-2) study,” Am. Heart J., 2003, 145:80-87.
Brown, N. et al., “Angiotensin-Converting Enzyme Inhibitors,” Circulation, 1998, 97:1411-1420.
Cushman, D. et al., “Design of potent competitive inhibitors of angiotensin-converting enzyme. Carboxyalkanoyl and mercaptoalkanoyl amino acids,” Biochemistry, 1977, 16:5484-5491.
Deddish, P. et al., “N-Domain-Specific Substrate and C-Domain Inhibitors of Angiotensin-Converting Enzyme: Angiotensin-(1-7) and Keto-ACE,” Hypertension, 1998, 31:912-917.
Georgiadis, D. et al., “Structural Determinants of RXPA380, a Potent and Highly Selective Inhibitor of the Angiotensin-Converting Enzyme C-Domain,” Biochemistry, 2004, 43:8048-8054.
Hvidt, T. et al., “Synthesis of enantiomerically pure β-amino-α-methylene-γ-butyrolactones by way of ozonolysis of aromatic α-amino acids,” Can. J. Chem., 1988, 66:779-782.
Israili, Z. et al., “Cough and Angioneurotic Edema Associated with Angiotensin-converting Enzyme Inhibitor Therapy: A Review of the Literature and Pathophysiology,” Annals of Internal Medicine, 1992, 117:234-242.
Natesh, R. et al., “Crystal structure of the human angiotensin-converting enzyme-lisinopril complex,” Nature, 2003, 421:551-554.
Natesh, R.. et al., “Structural Details on the Binding of Antihypertensive Drugs Captopril and Enalaprilat to Human Testicular Angiotensin I-Converting Enzyme,” Biochemistry, 2004, 43:8718-8724.
Ondetti, M. et al., “Design of Specific Inhibitors of Angiotensin-Converting Enzyme: New Class of Orally Active Antihypertensive Agents,” Science, 1977, 196:441-444.
Peng, S. et al., “Enantiomerically Pure Indoloquinolizines from Tryptophane,” Liebigs Ann. Chem., 1990, 313-318.
Raia, Jr. J. et al., “Angiotensin-Converting Enzyme Inhibitors: A Comparative Review,” DICP Ann. Pharmacother., 1990, 24:506-525.
Soubrier, F. et al., “Two putative active centers in human angiotensin I-converting enzyme revealed by molecular cloning,” Proc. Natl. Acad. Sci. USA., 1988, 85:9386-9390.
Peach, M., “Renin-Angiotensin System: Biochemistry and Mechanisms of Action,” Physiol. Rev., 1977, 57:313-370.
Ehlers, M. et al., “Angiotensin-Converting Enzyme: New Concepts Concerning Its Biological Role,” Biochemistry, 1989, 28:5311-5318.
Meyer, R. et al., “Novel Synthesis of (S)-1[5-(Benzoylamino)-1,4-dioxo-6-phenylhexyl]-L-proline and Analogues: Potent Angiotensin Converting Enzyme Inhibitors,” J. Med. Chem., 1981, 24:964-969.
Gonzalez-Muniz, R. et al., “Ketomethylene and (Cyanomethylene)amino Pseudopeptide Analogues of the C-Terminal Hexapeptide of Neurotensin,” J. Med. Chem., 1995, 38:1015-1021.
Garcia-Lopez, M.T. et al., “A Simple and Versatile Route to Ketomethylene Dipetide Analogs,” Tetrahedron Letters, 1988, 29:1577-1580.
Garcia-Lopez, M.T. et al., “Synthesis of Ketomethylene Dipetides Containing Basic Amino Acid Analogues at C-Terminus,” Tetradron, 1988, 44:5131-5138.
Kelly, T.R. et al., “A Convenient Preparation of Methyl and Ethyl Gloyoxylate,” Synthesis, 1972, 544-545.
Accelyrs-Additional Products, available at http://accelrys.com/products/additional-products.html printed as of Oct. 16, 2009.
Benedetti, F. et al., “Versatile and Stereoselective Synthesis of Diamino Diol Dipeptide Isosteres, Core Units of Pseudopeptide HIV Protease Inhibitors,” J. Org. Chem., 1997, 62:9348-9353.
Benedetti, F. et al., “Stereoselective Synthesis of Non Symmetric Dihydroxyethylene Dipeptide Isosteres Via Epoxyalcohols Derived From α-Amino Acids,” Bioorganic & Medicinal Chemistry Letters, 1999, 9:3027-3030.
Benedetti, F. et al., “New synthesis of 5-amino-4-hydroxy-2,6-dimethylheptanoic acid, a hydroxyethylene isostere of the Val-Ala dipeptide,” Tetrahedron Letters, 2000, 41:10075-10078.
Bersanetti, P. et al., “Positional-Scanning Combinatorial Libraries of Fluorescence Resonance Energy Transfer Peptides for Defining Substrate Specificity of the Angiotensin I-Converting Enzyme and Development of Selective C-Domain Substrates,” Biochemistry, 2004, 43:15729-15736.
Buikema, H., “Angiotensin-converting enzyme inhibitors zofenopril and lisinopril are both safe in the treatment of acute myocardial infarction,” Evidence-based Cardiovascular Medicine, 2003, 7:131-132.
Da, C. et al., “A convenient synthesis of piperidine-based β-amino alcohols from L-Phe and highly enantioselective addition of diethyl zinc to aldehydes,” Tetrahedron: Asymmetry, 2003, 14:659-665.
Deziel, R. et al., “A Practical and Diastereoselective Synthesis of Ketomethylene Dipeptide Isosteres of the Type AAψ[COCH2]Asp,” J. Org. Chem., 1996, 61:2901-2903.
Erdos, E., “Conversion of Angiotensin I to Angiotensin II,” Am. J. Med., 1976, 60:749-759.
Ghosh, A. et al., “Transition-State Mimetics for HIV Protease Inhibitors: Stereocontrolled Synthesis of Hydroxyethylene and Hydroxyethylamine Isosteres by Ester-Derived Titanium Enolate Syn and Anti-Aldol Reactions,” J. Org. Chem., 1998, 63:6146-6152.
Nchinda, A. et al., “Synthesis and molecular modeling of a lisinopril-tryptophan analogue inhibitor of angiotensin I-converting enzyme,” Biorganic & Medicinal Chemistry Letters, 2006, 16:4616-4619.
Skeggs, L. et al., “The Preparation and Function of the Hypertensin-Converting Enzyme,” J. Exp. Med., 1956, 103:295-299.
Tossi, A. et al., “Small hydroxyethylene-based peptidomimetics inhibiting both HIV-1 andC. albicansaspartic proteases,” Bioorganic & Medicinal Chemistry, 2003, 11:4719-4727.
International Search Report mailed Dec. 12, 2006 corresponding to Application No. PCT/IB2006/001411.
Written Opinion of the International Searching Authority mailed Dec. 19, 2007 corresponding to Application No. PCT/IB2006/001411.
Chibale Kelly
Nchinda Aloysius
Sturrock Edward
Hui San-ming
Kilpatrick Townsend & Stockton LLP
University of Cape Town
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