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Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

Thrombin Inhibition by the Highly Selective ‘ Reversible Suicide Substrate ’ N-Ethoxycarbonyl-D-Phenylalanyl-L-Prolyl-α-Azalysine p-Nitrophenyl Ester

Author(s): Paolo Ascenzi, Carlo Gallina and Martino Bolognesi

Volume 12, Issue 5, 2005

Page: [433 - 438] Pages: 6

DOI: 10.2174/0929866054395301

Price: $65

Abstract

Thrombin is the last enzyme in the blood coagulation cascade. All pharmacological aspects support the use of thrombin inhibitors as antithrombotic agents. Here, we review the unusual inhibition behavior of the highly selective reversible suicide substrate N-ethoxycarbonyl-D-phenylalanyl-L-prolyl-α-azalysine p-nitrophenyl ester (Eoc-D-Phe-ProazaLys- ONp) targeted to the active center of human a-thrombin. Eoc-D-Phe-Pro-azaLys-ONp is an acylating agent, but its hydrolysis product 1(N-ethoxycarbonyl-D-phenylalanyl-L-prolyl)-2(4-aminobutyl) hydrazine behaves as a highly selective human α-thrombin competitive inhibitor.

Keywords: human thrombin, catalytic and inhibition mechanism, substrate and inhibitor recognition, suicide substrate, structural aspects, kinetics, thermodynamics


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