Kulikov O V, Badelin V G, Krestov G A
Biofizika. 1993 Mar-Apr;38(2):213-21.
Peculiarities of intermolecular interactions in water-dimethylsulfoxide solutions of dipeptides-glycyl-glycine, beta-alanyl-glycine, beta-alanyl-beta-alanine, DL-alpha-alanyl-DL-alpha-alanine, DL-alpha-alanyl-DL-valine-were analysed on the basis of thermodynamic characteristics and data on IR-spectra. Dimethylsulfoxide additions were shown to cause destruction of peptide associates present in aqueous solutions due to the formation of stronger bonds "peptide-DMSO". The existence of complexes between dimethylsulfoxide and beta-alanyl-glycine, beta-alanyl-beta-alanine, DL-alpha-alanyl-DL-alpha-alanine was found. The mechanism of their formation was determined by the dipeptide structure.
基于热力学特性和红外光谱数据，分析了二肽（甘氨酰甘氨酸、β-丙氨酰甘氨酸、β-丙氨酰β-丙氨酸、DL-α-丙氨酰-DL-α-丙氨酸、DL-α-丙氨酰-DL-缬氨酸）在水-二甲基亚砜溶液中的分子间相互作用特性。结果表明，添加二甲基亚砜会导致水溶液中存在的肽缔合体被破坏，这是由于形成了更强的“肽-二甲基亚砜”键。发现二甲基亚砜与β-丙氨酰甘氨酸、β-丙氨酰β-丙氨酸、DL-α-丙氨酰-DL-α-丙氨酸之间存在络合物。其形成机制由二肽结构决定。
