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Ligand Preorganization May Be Accompanied by Entropic Penalties in Protein–Ligand Interactions
Author(s) -
Benfield Aaron P.,
Teresk Martin G.,
Plake Hilary R.,
DeLorbe John E.,
Millspaugh Laura E.,
Martin Stephen F.
Publication year - 2006
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.200600844
Subject(s) - ligand (biochemistry) , chemistry , derivative (finance) , computer science , receptor , combinatorial chemistry , computational biology , biochemistry , biology , business , finance
Fact or fiction? It is generally assumed that preorganization of a flexible ligand in the 3D shape it adopts when bound to a macromolecular receptor will provide a derivative with an increased binding affinity that benefits entropically (see picture). Contrary to this fundamental tenet of molecular recognition, it is shown that ligand preorganization in biological systems does not necessarily have a favorable entropic component.