| Literature DB >> 25919404 |
Jindřich Fanfrlík1, Francesc X Ruiz2, Aneta Kadlčíková1, Jan Řezáč1, Alexandra Cousido-Siah2, André Mitschler2, Susanta Haldar1, Martin Lepšík1, Michal H Kolář1,3, Pavel Majer1, Alberto D Podjarny2, Pavel Hobza1,4.
Abstract
The effect of halogen-to-hydrogen bond substitution on the binding energetics and biological activity of a human aldose reductase inhibitor has been studied using X-ray crystallography, IC50 measurements, advanced binding free energy calculations, and simulations. The replacement of Br or I atoms by an amine (NH2) group has not induced changes in the original geometry of the complex, which made it possible to study the isolated features of selected noncovalent interactions in a biomolecular complex.Entities:
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Year: 2015 PMID： 25919404 DOI： 10.1021/acschembio.5b00151
Source DB: PubMed Journal: ACS Chem Biol ISSN： 1554-8929 Impact factor: 5.100