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Thermodynamic Inhibition Profile of a Cyclopentyl and a Cyclohexyl Derivative towards Thrombin: The Same but for Different Reasons
Author(s) -
Gerlach Christof,
Smolinski Michael,
Steuber Holger,
Sotriffer Christoph A.,
Heine Andreas,
Hangauer David G.,
Klebe Gerhard
Publication year - 2007
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200701169
Subject(s) - thrombin , chemistry , derivative (finance) , thermodynamics , constant (computer programming) , stereochemistry , computational chemistry , medicinal chemistry , physics , economics , computer science , medicine , platelet , financial economics , programming language
Small changes, big effects : Two thrombin inhibitors (see picture; R=cyclopentyl ( 1 a ), R=cyclohexyl ( 1 b )) were characterized thermodynamically and computationally to explain their identical binding constants. Surprisingly, the free energy of binding is achieved with different enthalpic and entropic contributions (see plot).