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Design of Novel, Nonpeptidic Thrombin Inhibitors and Structure of a Thrombin–Inhibitor Complex
Author(s) -
Obst Ulrike,
Gramlich Volker,
Diederich François,
Weber Lutz,
Banner David W.
Publication year - 1995
Publication title -
angewandte chemie international edition in english
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 0570-0833
DOI - 10.1002/anie.199517391
Subject(s) - thrombin , serine protease , active site , coagulation , chemistry , discovery and development of direct thrombin inhibitors , enzyme inhibitor , protease inhibitor (pharmacology) , stereochemistry , enantiomer , enzyme , protease , biochemistry , platelet , biology , medicine , immunology , human immunodeficiency virus (hiv) , antiretroviral therapy , viral load
A strong inhibition of the serine protease thrombin , important in the blood coagulation process, was achieved through de novo designed inhibitors. The most active compound is shown. The X‐ray crystal structure of the thrombin–inhibitor complex showed the binding mode of these compounds and confirmed that only the enantiomer predicted by computer modeling was bound in the active site.