オリゴペプチドの疎水性の解析と予測

概要

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The log P value used for the hydrophobicity parameter, where P is the partition coefficient in a 1-octanol/pH 7.0 buffer system, of a number of di-pentapeptides was analyzed with physicochemical parameters for the side chain substituent of component amino acids. The log P value was shown to be governed not only by the “intrinsic” hydrophobicity but also by the steric effect of side chain substituents as well as intramolecular-type solvation and “polar proximity” effects for polar side chains. The β-turn conformational parameters of component amino acids devised from the Chou-Fasman propensity index were nicely applied for the analysis of log P value of tetra-and pentapeptides.Using the results of the correlation analyses for log P of oligopeptides, we proposed a new effective hydrophobicity scale, π<SUB>α</SUB>, for unionizable amino acid side chains. This scale and the hydrophobicity of oligopeptides would be useful not only for the process of peptide synthesis but also for the quantitative analysis of the structure-activity relationship of bioactive peptides.
社団法人有機合成化学協会の論文