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Systematic Investigation of Halogen Bonding in Protein–Ligand Interactions
Author(s) -
Hardegger Leo A.,
Kuhn Bernd,
Spinnler Beat,
Anselm Lilli,
Ecabert Robert,
Stihle Martine,
Gsell Bernard,
Thoma Ralf,
Diez Joachim,
Benz Jörg,
Plancher JeanMarc,
Hartmann Guido,
Banner David W.,
Haap Wolfgang,
Diederich François
Publication year - 2011
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.201006781
Subject(s) - halogen bond , halogen , chemistry , ligand (biochemistry) , aryl , atom (system on chip) , ring (chemistry) , covalent bond , fluorine , crystallography , stereochemistry , organic chemistry , biochemistry , computer science , receptor , alkyl , embedded system
Halogen bonding triggers activity : Increasing binding affinity was observed for a series of covalent human Cathepsin L inhibitors by exchanging an aryl ring H atom with Cl, Br, and I, which undergo halogen bonding with the CO group of Gly61 in the S3 pocket of the enzyme. Fluorine, in contrast, strongly avoids halogen bonding (see scheme). The strong distance and angle dependence of halogen bonding was confirmed for biological systems.