β-内啡肽：脂质溶液中α-螺旋的形成
beta-Endorphin: formation of alpha-helix in lipid solutions.
作者信息
Wu C S, Lee N M, Loh H H, Yang J T, Li C H
出版信息
Proc Natl Acad Sci U S A. 1979 Aug;76(8):3656-9. doi: 10.1073/pnas.76.8.3656.
Abstract
Human beta-endorphin adopts a partial helical conformation in aqueous solutions of cerebroside sulfate, ganglioside GM1, phosphatidylserine, and phosphatidic acid, but not of cerebroside and phosphatidylcholine, as evidenced by circular dichroic spectra. Addition of Ca2+ to the peptide in cerebroside sulfate solution can break up the helix; at 10 mM Ca2+ the peptide (12 microM) essentially exists in an unordered form. For comparison, sheep beta-lipotropin in acidic cerebroside sulfate solution (pH less than 4) also has a partial helical conformation of the complex between human beta-endorphin and lipids may be related to the opiatelike function of this peptide hormone.
摘要
圆二色光谱表明，人β-内啡肽在硫酸脑苷脂、神经节苷脂GM1、磷脂酰丝氨酸和磷脂酸的水溶液中呈部分螺旋构象，但在脑苷脂和磷脂酰胆碱的水溶液中则不然。向硫酸脑苷脂溶液中的肽添加Ca2+会破坏螺旋结构；在10 mM Ca2+时，该肽（12 μM）基本上以无序形式存在。相比之下，酸性硫酸脑苷脂溶液（pH小于4）中的绵羊β-促脂素也具有部分螺旋构象，人β-内啡肽与脂质之间的复合物可能与其作为肽类激素的阿片样功能有关。
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本文引用的文献
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