Cserháti T, Forgács E
Central Research Institute for Chemistry, Hungarian Academy of Sciences, Budapest, Hungary.
Biochem Mol Biol Int. 1995 Oct;37(3):555-62.
The interaction of amino acids with the cationic surfactant cetyltrimethylammoniumbromide (CTAB) was studied by charge transfer reversed-phase thin-layer chromatography and the relative strength of interaction was calculated. In the majority of cases the surfactant has a negligible effect on the hydrophobicity of amino acids. Only the binding of Arg, Glu, Gly, Leu, Lys, Met, Nle, Phe Trp, Tyr and Val to the surfactant was observed, however, the strength of interaction was fairly low. The hydrophobicity of the amino acid side chains significantly influenced the strength of interaction. The findings support the hypothesis that the binding of cationic surfactants to proteins involves more than one amino acid residues and that the hydrophobic forces have a considerable impact on the interaction.
通过电荷转移反相薄层色谱法研究了氨基酸与阳离子表面活性剂十六烷基三甲基溴化铵（CTAB）的相互作用，并计算了相互作用的相对强度。在大多数情况下，表面活性剂对氨基酸的疏水性影响可忽略不计。然而，仅观察到精氨酸、谷氨酸、甘氨酸、亮氨酸、赖氨酸、蛋氨酸、正亮氨酸、苯丙氨酸、色氨酸、酪氨酸和缬氨酸与表面活性剂的结合，但其相互作用强度相当低。氨基酸侧链的疏水性显著影响相互作用强度。这些发现支持了以下假设：阳离子表面活性剂与蛋白质的结合涉及多个氨基酸残基，并且疏水力对这种相互作用有相当大的影响。
