Premium
Heuristic molecular lipophilicity potential (HMLP): Lipophilicity and hydrophilicity of amino acid side chains
Author(s) -
Du QiShi,
Li DaPeng,
He WenZhang,
Chou KuoChen
Publication year - 2006
Publication title -
journal of computational chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.907
H-Index - 188
eISSN - 1096-987X
pISSN - 0192-8651
DOI - 10.1002/jcc.20369
Subject(s) - lipophilicity , chemistry , octanol , cyclohexane , van der waals force , side chain , computational chemistry , partition coefficient , molecular dynamics , stereochemistry , thermodynamics , molecule , organic chemistry , physics , polymer
Heuristic molecular lipophilicity potential (HMLP) is applied in the study of lipophilicity and hydrphilcity of 20 natural amino acids side chains. The HMLP parameters, surface area S i , lipophilic indices L i , and hydrophilic indices H i of amino acid side chains are derived from lipophilicity potential L (r). The parameters are correlated with the experimental data of phase‐transferring free energies of vapor‐to‐water, vapor‐to‐cyclohexane, vapor‐to‐octanol, cyclohexane‐to‐water, octanol‐to‐water, and cyclohexane‐to‐octanol through a linear free energy equation Δ G ° tr, i = b 0 + b 1 S i + + b 2 S i − + b 3 L i + b 4 H i . For all above six phase‐transfer free energies, the HMLP parameters of 20 amino acid side chains give good calculation results using linear free energy equation. HMLP is an ab initio quantum chemical approach and a structure‐based technique. Except for atomic van der Waals radii, there are no other empirical parameters used. The HMLP has clear physical and chemical meaning and provides useful lipophilic and hydrophilic parameters for the studies of proteins and peptides. © 2006 Wiley Periodicals, Inc. J Comput Chem 27: 685–692, 2006