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Structure‐Lipophilicity and Structure‐Polarity relationships of amino acids and peptides
Author(s) -
Vallat Philippe,
Gaillard Patrick,
Carrupt PierreAlain,
Tsai RueyShiuan,
Testa Bernard
Publication year - 1995
Publication title -
helvetica chimica acta
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.74
H-Index - 82
eISSN - 1522-2675
pISSN - 0018-019X
DOI - 10.1002/hlca.19950780218
Subject(s) - lipophilicity , chemistry , polarity (international relations) , side chain , amino acid , peptide , polar , stereochemistry , partition coefficient , organic chemistry , biochemistry , polymer , cell , physics , astronomy
Abstract The objectives of this study were to gain insights into the structure‐lipophilicity relationships of peptides and to propose an improved model for estimating their lipophilicity. First, existing databases were extended to obtain the distribution coefficients of a total of 208 free or protected peptides (di‐ to pentapeptides). The polarity parameters (Λ) of 23 free amino acids and 19 protected amino acids (AcNHCHRCONH 2 ) and of their side chains were calculated from experimental distribution coefficients and computed molecular volumes. An analysis of the polarity parameters revealed that the hydrophobicity of the amino‐acid side chains is largely reduced due to the polar field of the backbone. The polarity parameters of the peptides were then obtained in a similar manner and shown to be highly correlated with the sum of the polarity parameters of their side chains, i.e. , the lipophilicity of peptides can be calculated from their molecular volume and the sum of their side‐chain polarities using the regression established for each individual series of peptides ( Fig. 1 ). This last restriction is essential since the polarity and lipophilic increment of a NHC*HCO unit were shown to decrease with increasing length of backbone.

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