HYDROPHOBICITY OF PEPTIDES AND RELATED-COMPOUNDS .2. HYDROPHOBICITY OF N-ACETYL-DIPEPTIDE AND TRIPEPTIDE AMIDES HAVING UNIONIZABLE SIDE-CHAINS AND CORRELATION WITH SUBSTITUENT AND STRUCTURAL PARAMETERS
HYDROPHOBICITY OF PEPTIDES AND RELATED-COMPOUNDS .2. HYDROPHOBICITY OF N-ACETYL-DIPEPTIDE AND TRIPEPTIDE AMIDES HAVING UNIONIZABLE SIDE-CHAINS AND CORRELATION WITH SUBSTITUENT AND STRUCTURAL PARAMETERS
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DOI：
10.1002/qsar.19900090302
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发表时间：
1990-09-01
期刊：
影响因子：
--
通讯作者：
FUJITA, T
中科院分区：
文献类型：
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作者：
AKAMATSU, M;OKUTANI, S;FUJITA, T
在1-辛醇/pH 7.0的水性缓冲体系中测量了由具有不可电离侧链的氨基酸组成的53种N-乙酰基-二肽和三肽酰胺的log P值。这些保护肽之间的log P值的变化的因素进行了定量分析，制定一个与自由能相关的理化和亚结构参数的相关方程。log P值由侧链和主链的疏水性的总和以及侧链取代基对主链CONH基团的相对溶剂化的空间效应决定。在其他因素相同的情况下，发现肽键的log P值降低0.6 log单位。对于具有极性侧链的氨基酸，log P值也受到“极性邻近因子”和/或分子内氢键形成的影响，其方式类似于先前报道的两性离子化肽。
The log P value of 53 N-acetyl-di- and tripeptide amides composed of amino acids having unionizable side chains was measured in a 1-octanol/pH 7.0 aqueous buffer system. The factors governing the variations in the log P value among these protected peptides were quantitatively analyzed to formulate a correlation equation with free-energy-related physicochemical and substructural parameters. The log P value was governed by the sum of the hydrophobicity of side chains and the backbone as well as by the steric effects of side chain substituents on the relative solvation of the backbone CONH groups. The log P value was found to decrease by 0.6 log unit for the peptide bond, other factors being equal. For amino acids with polar side chains, the log P value was also affected by the "polar proximity factor" and/or intramolecular hydrogen bond formation in a way similar to that of zwitterionized peptides reported previously.