@article{ref1,
title="Thrombin inhibition by the highly selective 'reversible suicide substrate' N-ethoxycarbonyl-D-phenylalanyl-L-prolyl-alpha-azalysine p-nitrophenyl ester",
journal="Protein and peptide letters",
year="2005",
author="Ascenzi, Paolo and Gallina, Carlo and Bolognesi, Martino",
volume="12",
number="5",
pages="433-438",
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-alpha-azalysine p-nitrophenyl ester (Eoc-D-Phe-Pro-azaLys-ONp) targeted to the active center of human alpha-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 alpha-thrombin competitive inhibitor.<p /><p>Language: en</p>",
language="en",
issn="0929-8665",
doi="10.2174/0929866054395301",
url="http://dx.doi.org/10.2174/0929866054395301"
}