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Computational study of the molecular mechanisms of caffeine action: Caffeine complexes with adenosine receptors
Author(s) -
Poltev V. I.,
Rodríguez E.,
Grokhlina T. I.,
Deriabina A.,
Gonzalez E.
Publication year - 2009
Publication title -
international journal of quantum chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.484
H-Index - 105
eISSN - 1097-461X
pISSN - 0020-7608
DOI - 10.1002/qua.22106
Subject(s) - adenosine receptor , chemistry , caffeine , molecular mechanics , adenosine , transmembrane protein , receptor , transmembrane domain , molecule , mutagenesis , molecular model , stereochemistry , hydrogen bond , amino acid , biophysics , molecular dynamics , computational chemistry , biochemistry , organic chemistry , biology , gene , agonist , endocrinology , mutation
To understand the molecular basis of the principal biological action of the caffeine (CAF), the molecular mechanics calculations of possible complexes between CAF and the fragments of human A 1 adenosine receptor were performed. The fragments were selected after considerations of the CAF molecular structure and its possible interactions, as well as after an analysis of the extensive bibliography on the structure, biological role, site‐directed mutagenesis, and the modeling of the adenosine receptors. The minimum energy configurations of these complexes were obtained using two different computer programs with different force fields. The most favorable configurations correspond to the formation of two hydrogen bonds between the CAF molecule and hydrophilic amino acid residues of the fragments of transmembrane domains of the receptor. These configurations are supposed to contribute to CAF blocking of the adenosine receptors. They will be used later for the construction of model CAF complexes with two transmembrane domains simultaneously. © 2009 Wiley Periodicals, Inc. Int J Quantum Chem, 2010