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Similar but Different: Thermodynamic and Structural Characterization of a Pair of Enantiomers Binding to Acetylcholinesterase
Author(s) -
Berg Lotta,
Niemiec Moritz S.,
Qian Weixing,
Andersson C. David,
WittungStafshede Pernilla,
Ekström Fredrik,
Linusson Anna
Publication year - 2012
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.201205113
Subject(s) - enantiomer , acetylcholinesterase , hydrogen bond , non covalent interactions , chemistry , ligand (biochemistry) , affinities , binding affinities , stereochemistry , acetylcholinesterase inhibitor , computational biology , combinatorial chemistry , crystallography , biochemistry , enzyme , biology , molecule , organic chemistry , receptor
Take a closer look: Unexpectedly, a pair of enantiomeric ligands proved to have similar binding affinities for acetylcholinesterase. Further studies indicated that the enantiomers exhibit different thermodynamic profiles. Analyses of the noncovalent interactions in the protein–ligand complexes revealed that these differences are partly due to nonclassical hydrogen bonds between the ligands and aromatic side chains of the protein.