Macrocyclic inhibitors for the serine protease plasmin

References

• MD Sternlicht, Z Werb. How matrix metalloproteinases regulate cell behavior. Annu Rev Cell Dev Biol 2001;17:463–516.
   PubMed Web of Science ®Google Scholar
• H Nagase, JF WoessnerJr. Matrix metalloproteinases. J Biol Chem 1999;274:21491–21494.
   PubMed Web of Science ®Google Scholar
• P Mignatti, DB Rifkin. Plasminogen activators and matrix metalloproteinases in angiogenesis. Enzyme Protein 1996;49:117–137. (b) Murphy G, Stanton H, Cowell S, Butler G, Knauper V, Atkinson S, Gavrilovic J. Mechanisms for pro matrix metalloproteinase activation. Acta Pathol Mic Sc 1999;107:38–44
   PubMedGoogle Scholar
• PM Mannucci. Hemostatic drugs. N Engl J Med 1998;339:245–253.
   PubMed Web of Science ®Google Scholar
• JL Conroy, TC Sanders, CT Seto. Using the electrostatic field effect to design a new class of inhibitors for cysteine proteases. J Am Chem Soc 1997;119:4285–4291. (b) Conroy JL, Seto CT. 13C NMR studies demonstrate that tetrahydropyranone-based inhibitors bind to cysteine proteases by reversible formation of a hemithioketal adduct. J Org Chem 1998;63:2367–2370. (c) Abato P, Yuen CM, Cubanski JY, Seto CT. Inhibitors of plasmin that extend into both the S and S′ binding sites: cooperative interactions between S1 and S2. J Org Chem 2002;67:1184–1191. (d) Abato P, Conroy JL, Seto CT. A combinatorial library of serine and cysteine protease inhibitors that interact with both the S and S′ binding sites. J Med Chem 1999;42:4001–4009. (e) Xue F, Seto CT. A comparison of cyclohexanone and tetrahydro-4H-thiopyran-4-one 1,1-dioxide as pharmacophores for the design of peptide-based inhibitors of the serine protease plasmin. J Org Chem 2005:70:8309–8321. (f) Xue F, Seto CT. Selective inhibitors of the serine protease plasmin: probing the S3 and S3′ subsites using a combinatorial library. J Med Chem 2005;68:6908–6917. (g) Xue F, Seto CT. Structure-activity studies of cyclic ketone inhibitors of the serine protease plasmin: Design, synthesis and biological activity. Bioorg Med Chem 2006;14:8467–8487. (h) Sanders TC, Seto CT. 4-Heterocyclohexanone-based inhibitors of the serine protease plasmin. J Med Chem 1999;42:2969–2976
   Web of Science ®Google Scholar
• WA Loughlin, JDA Tyndall, MP Glenn, DP Fairlie. Beta-strand mimetics. Chem Rev 2004;104:6085–6117. (b) Tyndall JDA, Nall T, Fairlie DP. Proteases universally recognize beta strands in their active sites. Chem Rev 2005;105:973–999. (c) Tyndall JD, Fairlie DP. Macrocycles mimic the extended peptide conformation recognized by aspartic, serine, cysteine and metallo proteases. Curr Med Chem 2001;8:893–907
   PubMed Web of Science ®Google Scholar
• JW Janetka, P Raman, K Satyshur, GR Flentke, DH Rich. Novel cyclic biphenyl ether peptide β-strand mimetics and HIV-protease inhibitors. J Am Chem Soc 1997;119:441–442.
   Web of Science ®Google Scholar
• RC Reid, DR March, MJ Dooley, DA Bergman, G Abbenante, DP Fairlie. A novel bicyclic enzyme inhibitor as a consensus peptido-mimetic for the receptor-bound conformations of twelve peptidic inhibitors of HIV-1 protease. J Am Chem Soc 1996;118:8511–8517.
   Web of Science ®Google Scholar
• KX Chen, FG Njoroge, J Pichardo, A Prongay, N Butkiewicz, N Yao, V Madison, V Girijavallabhan. Potent 7-hydroxy-1,2,3,4-tetrahydroisoquinoline-3-carboxylic acid-based macrocyclic inhibitors of hepatitis C virus NS3 protease. J Med Chem 2006;49:567–574.
   PubMed Web of Science ®Google Scholar
• YS Tsantrizos, J-M Ferland, A McClory, M Poirier, V Farina, NK Yee, X Wang, N Haddad, X Wei, J Xu, L Zhang. Olefin ring-closing metathesis as a powerful tool in drug discovery and development - potent macrocyclic inhibitors of the hepatitis C virus NS3 protease. J Organomet Chem 2006;691:5163–5171.
   Web of Science ®Google Scholar
• JH Meyer, PA Bartlett. Macrocyclic inhibitors of penicillopepsin 1. Design, synthesis, and evaluation of an inhibitor bridged between P1 and P3. J Am Chem Soc 1998;120:4600–4609.
   Web of Science ®Google Scholar
• SJ Stachel, CA Coburn, S Sankaranarayanan, EA Price, BL Pietrak, Q Huang, J Lineberger, AS Espeseth, X Jin, J Elis, MK Holloway, S Munshi, T Allison, D Hazuda, AJ Simon, SL Graham, JP Vacca. Macrocyclic inhibitors of β-secretase: functional activity in an animal model. J Med Chem 2006;49:6147–6150.
   PubMed Web of Science ®Google Scholar
• CB Xue, ME Voss, DJ Nelson, JJ Duan, RJ Cherney, IC Jacobson, X He, J Roderick, L Chen, RL Corbett, L Wang, DT Meyer, K Kennedy, WF DeGradodagger, KD Hardman, CA Teleha, BD Jaffee, RQ Liu, RA Copeland, MB Covington, DD Christ, JM Trzaskos, RC Newton, RL Magolda, RR Wexler, CP Decicco. Design, synthesis, and structure-activity relationships of macrocyclic hydroxamic acids that inhibit tumor necrosis factor α release in vitro and in vivo. J Med Chem 2001;44:2636–2660.
   PubMed Web of Science ®Google Scholar
• S Thaisrivongs, DT Pals, SR Turner, LT Kroll. Conformationally constrained renin inhibitory peptides: γ-lactam-bridged dipeptide isostere as conformational restriction. J Med Chem 1988;31:1369–1376.
   PubMed Web of Science ®Google Scholar
• Y Okada, Y Tsuda, N Teno, K Wanaka, M Bohgaki, A Hijikata-Okunomiya, T Naito, S Okamoto. Synthesis of active center-directed peptide inhibitors of plasmin. Chem Pharm Bull 1988;36:1289–1297, (b) S Okamoto, S Sato, Y Tanaka, U Okamoto. An active stereoisomer (trans form) of AMCHA and its antifibrinolytic (antiplasminic) action in vitro and in vivo. Keio J Med 1964;13:177–185.
   PubMed Web of Science ®Google Scholar