Asao M, Iwamura H, Akamatsu M, Fujita T
Department of Agricultural Chemistry, Faculty of Agriculture, Kyoto University, Japan.
J Med Chem. 1987 Oct;30(10):1873-9. doi: 10.1021/jm00393a031.
Bitter thresholds of a total of 93 amino acids, peptides, and their derivatives were analyzed quantitatively by use of hydrophobicity parameters reported for amino acid side chains and those for the whole molecules estimated from partition coefficients obtained experimentally. We also explored the steric parameters that best explained the variation in the intensity of bitterness attributable to the molecular shape. The results showed that the total length along the zigzag peptide backbone chain of the molecule is an important factor. The bitterness of nonzwitterionic N-acyl and ester derivatives and that of neutral N-acyl ester derivatives were expressed by a single, common equation together with those of zwitterionic amino acids and peptides. Thus the interaction via the charge with the receptor site was probably not an indispensible factor for triggering of the bitter sensation. This study, together with earlier ones, may serve as a prototype of approaches toward unraveling structure-activity relationships of complex molecules like amino acids, peptides, and their derivatives that are of medicinal or agricultural importance.
利用已报道的氨基酸侧链疏水性参数以及根据实验获得的分配系数估算的整个分子的疏水性参数，对总共93种氨基酸、肽及其衍生物的苦味阈值进行了定量分析。我们还探索了最能解释因分子形状导致的苦味强度变化的空间参数。结果表明，分子沿锯齿状肽主链的总长度是一个重要因素。非两性离子型N-酰基和酯衍生物以及中性N-酰基酯衍生物的苦味与两性离子型氨基酸和肽的苦味由一个共同的方程表示。因此，通过电荷与受体位点的相互作用可能不是引发苦味感觉的不可或缺的因素。这项研究与早期的研究一起，可能成为揭示氨基酸、肽及其衍生物等具有医学或农业重要性的复杂分子的构效关系方法的原型。
