Tripeptides with non-code amino acids as potential serine proteases inhibitors

References

• Nduwimana J, Guenet L, Dorval I, Blayau M, Le Gall JY, Le Treut A. Proteases. Ann Biol Clin (Paris) 1995;53:251–264.
   PubMedGoogle Scholar
• Longstaff C, Thelwell C. Understanding the enzymology of fibrinolysis and improving thrombolytic therapy. FEBS Lett 2005;579:3303–3309.
   PubMedGoogle Scholar
• Hervio LS, Coombs GS, Bergstrom RC, Trivedi K, Corey DR, Madison EL. Negative selectivity and the evolution of protease cascades: the specificity of plasmin for peptide and protein substrates. Chem Biol 2000;7:443–453.
   PubMedGoogle Scholar
• Gechtman Z, Sharma R, Kreizman T, Fridkin M, Shaltiel S. Synthetic peptides derived from the sequence around the plasmin cleavage site in vitronectin. Use in mapping the PAI-1 binding site. FEBS Lett 1993;315:293–297.
   PubMedGoogle Scholar
• Backes BJ, Harris JL, Leonetti F, Craik CS, Ellman JA. Synthesis of positional-scanning libraries of fluorogenic peptide substrates to define the extended substrate specificity of plasmin and thrombin. Nat Biotechnol 2000;18:187–193.
   PubMed Web of Science ®Google Scholar
• Tsuda Y, Teno N, Okada Y, Wanaka K, Bohgaki M, Hijikata-Okunomiya A et al. Synthesis of tripeptide chloromethyl ketones and examination of their inhibitory effects on plasmin and plasma kallikrein. Chem Pharm Bull 1989;37:3108–3111.
   PubMedGoogle Scholar
• Markowska A, Bruzgo I, Midura-Nowaczek K. Methylketone inhibitors of plasmin. Pharmazie 2006;61:898–900.
   PubMedGoogle Scholar
• Markowska A, Midura-Nowaczek K, Bruzgo I. Low molecular peptides as potential inhibitors of plasmin. Acta Pol Pharm 2007;64:355–358.
   PubMedGoogle Scholar
• Weitz JI. A novel approach to thrombin inhibition. Thromb Res 2003;109:S17–S22.
   PubMedGoogle Scholar
• Altenburger JM, Lassalle GY, Matrougui M, Galtier D, Jetha JC, Bocskei Z et al. SSR182289A, a selective and potent orally active thrombin inhibitor. Bioorg Med Chem 2004;12:1713–1730.
   PubMed Web of Science ®Google Scholar
• Olsen JV, Ong SE, Mann M. Trypsin cleaves exclusively C-terminal to arginine and lysine residues. Mol Cell Proteomics 2004;3:608–614.
   PubMed Web of Science ®Google Scholar
• Navaneetham D, Sinha D, Walsh PN. Mechanisms and specificity of factor XIa and trypsin inhibition by protease nexin 2 and basic pancreatic trypsin inhibitor. J Biochem 2010;148:467–479.
   PubMedGoogle Scholar
• Ke SH, Coombs GS, Tachias K, Corey DR, Madison EL. Optimal subsite occupancy and design of a selective inhibitor of urokinase. J Biol Chem 1997;272:20456–20462.
   PubMed Web of Science ®Google Scholar
• Duffy MJ. The urokinase plasminogen activator system: role in malignancy. Curr Pharm Des 2004;10:39–49.
   PubMed Web of Science ®Google Scholar
• Schweinitz A, Steinmetzer T, Banke IJ, Arlt MJ, Stürzebecher A, Schuster O et al. Design of novel and selective inhibitors of urokinase-type plasminogen activator with improved pharmacokinetic properties for use as antimetastatic agents. J Biol Chem 2004;279:33613–33622.
   PubMed Web of Science ®Google Scholar
• Markowska A, Bruzgo I, Midura-Nowaczek K. Effects of tripeptides on the amidolytic activities of urokinase thrombin, plasmin and trypsin. Int J Pept Res Ther 2008;14:215–218.
   Web of Science ®Google Scholar
• Markowska A, Bruzgo I, Midura-Nowaczek K. Synthesis and activity of amides of tripeptides as potential urokinase inhibitors. J Enzyme Inhib Med Chem 2010;25:139–142.
   PubMed Web of Science ®Google Scholar
• Markowska A, Bruzgo I, Miltyk W, Midura-Nowaczek K. Synthesis and activity of N-sulfonylamides of tripeptides as potential urokinase inhibitors. Protein Pept Lett 2010;17:1300–1304.
   PubMedGoogle Scholar
• Markowska A, Bruzgo I, Miltyk W, Midura-Nowaczek K. Tripeptides with C-Terminal Arginine as Potential Inhibitors of Urokinase. Int J Pept Res Ther 2011;17:47–52.
   Google Scholar
• Harmat NJ, Di Bugno C, Criscuoli M, Giorgi R, Lippi A, Martinelli A et al. 1,2-disubstituted cyclohexane derived tripeptide aldehydes as novel selective thrombin inhibitors. Bioorg Med Chem Lett 1998;8:1249–1254.
   PubMedGoogle Scholar
• Chan WC, White PD. Fmoc Solid Phase Peptide Synthesis. Oxford University Press: New York 2000.
   Google Scholar
• Okada Y, Tsuda Y, Teno N, Wanaka K, Bohgaki M, Hijikata-Okunomiya A et al. Synthesis of active center-directed peptide inhibitors of plasmin. Chem Pharm Bull 1988;36:1289–1297.
   PubMed Web of Science ®Google Scholar
• Cheng Y, Prusoff WH. Relationship between the inhibition constant (K1) and the concentration of inhibitor which causes 50 per cent inhibition (I50) of an enzymatic reaction. Biochem Pharmacol 1973;22:3099–3108.
   PubMed Web of Science ®Google Scholar
• Aoyagi T, Miyata S, Nanbo M, Kojima F, Matsuzaki M. Biological activities of leupeptins. J Antibiot 1969;22:558–568.
   PubMed Web of Science ®Google Scholar
• Plumb JA, Milroy R, Kaye SB. Effects of the pH dependence of 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyl-tetrazolium bromide-formazan absorption on chemosensitivity determined by a novel tetrazolium-based assay. Cancer Res 1989;49:4435–4440.
   PubMed Web of Science ®Google Scholar
• Tsuda Y, Tada M, Wanaka K, Okamoto U, Hijikata-Okunomiya A, Okamoto S et al. Structure-inhibitory activity relationship of plasmin and plasma kallikrein inhibitors. Chem Pharm Bull 2001;49:1457–1463.
   PubMedGoogle Scholar
• Enomoto R, Sugahara C, Komai T, Suzuki C, Kinoshita N, Hosoda A et al. The structure-activity relationship of various YO compounds, novel plasmin inhibitors, in the apoptosis induction. Biochim Biophys Acta 2004;1674:291–298.
   PubMedGoogle Scholar
• Lynas JF, Martin SL, Walker B. Synthesis and kinetic evaluation of peptide α-keto-β-aldehyde-based inhibitors of trypsin-like serine proteases. J Pharm Pharmacol 2001;53:473–480.
   PubMedGoogle Scholar
• Stillfried GE, Saunders DN, Ranson M. Plasminogen binding and activation at the breast cancer cell surface: the integral role of urokinase activity. Breast Cancer Res 2007;9:R14.
   PubMedGoogle Scholar