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Ab initio studies on the binding of Na + and K + to the fundamental components of depsipeptides
Author(s) -
Pullman Alberte
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.560080707
Subject(s) - amide , depsipeptide , affinities , chemistry , ab initio , binding affinities , peptide , computational chemistry , stereochemistry , crystallography , organic chemistry , receptor , biochemistry
It is shown that the relative intrinsic affinities of the amide and ester carbonyl groups are larger for Na + than for K + (like the affinity of water), that the affinity of the amide for the two cations is larger than that of the ester, that the preferred position of the cation is in the plane of the peptide or ester bond at about 35 degrees of CO (toward the C x ) with very easy in‐plane displacements. The essential electrostatic nature of the binding and the small weight of the charge‐transfer effect are assessed. Implications for the functioning of depsipeptides as cation‐carrier are discussed.