Lipid‐induced conformational changes in glucagon, secretin, and vasoactive intestinal peptide
Lipid‐induced conformational changes in glucagon, secretin, and vasoactive intestinal peptide
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脂质诱导的胰高血糖素、促胰液素和血管活性肠肽的构象变化
DOI：
10.1002/bip.360210615
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发表时间：
1982
期刊：
影响因子：
2.9
通讯作者：
W. Mattice
中科院分区：
文献类型：
--
作者：
R. M. Robinson;E. Blakeney;W. Mattice
本文研究了胰高血糖素、促胰液素和血管活性肠肽在水和十二烷基硫酸酯、磷脂酰甘油和L-α-磷脂酸(二棕榈酰基)水溶液中的CD随温度的变化。阴离子洗涤剂和脂类在所有三种多肽中诱导螺旋形成，诱导的螺旋含量按胰高血糖素、促胰液素和血管活性肠肽的顺序增加。使用配置分配函数的矩阵公式对这些观察结果进行定量合理化。在该配方中，与阴离子脂类或洗涤剂相互作用的主要构象结果是精氨基、组氨基和赖氨基残基形成螺旋的可能性增加。在所有三种多肽中，螺旋形成最多的区域都在氨基酸残基13-20处。其他研究表明，多肽链的这一部分与受体结合有关。因此，与阴离子脂类相互作用所诱导的螺旋片段可能起着重要的生理作用。
The CD of glucagon, secretin, and vasoactive intestinal peptide has been studied as a function of temperature in water and in aqueous solutions of dodecyl sulfate, phosphatidyl glycerol, and L‐α‐phosphatidic acid (dipalmitoyl). The anionic detergent and lipids induce helix formation in all three peptides, with the amount of induced helical content increasing in the order glucagon < secretin < vasoactive intestinal peptide. These observations are subject to quantitative rationalization using a matrix formulation for the configuration partition function. In this formulation the major conformational consequences of the interaction with anionic lipids or detergents is an increase in the probability for helix formation by arginyl, histidyl, and lysyl residues. The region in which helix formation is maximal is found to be at amino acid residues 13–20 in all three peptides. Other studies have implicated this portion of the polypeptide chain in receptor binding. Thus, the helical segment induced by interaction with anionic lipids may play an important physiological role.