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化学学报
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化学学报 ›› 1997, Vol. 55 ›› Issue (2): 184-188. 上一篇    下一篇

研究论文

光谱法研究钙调素与蜂毒肽片断及其类似物的相互作用

阎虎生;刘利平;程晓辉;何炳林   

  1. 南开大学高分子化学研究所
  • 发布日期:1997-02-15

Study on the interaction of deletion peptide of melittin and its agalogs with calmodulin through spectral methods

YAN HUSHENG;LIU LIPING;CHENG XIAOHUI;HE BINGLIN   

  • Published:1997-02-15

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419

被引次数

1

设计合成了蜂毒肽片断及其类似物: Mel15, Mel15(8F)和Mel15(7P), 这些多肽与钙调素有很强的结合力, 而且链段很短, 因此它们可作为钙调素可结合蛋白质的结合部位的模型。本文采用光谱法研究了它们与钙调素的相互作用。荧光发射光谱法结果表明, 多肽Mel15在与钙调素相互作用时, 肽链中的Trp基团的微环境变得更加疏水, 说明Mel15中的Trp残基可能与钙调素的疏水性表面靠近。紫外差谱测试表明, 只有当钙调素分子结合2个Ca^2^+后, 才可以与多肽Mel15(8F)结合。圆二色谱法研究表明, 多肽与钙调素结合后多肽分子和钙调素分子的α-螺旋结构的含量都被诱导而增加, 结合力越大, 则越多的残基被诱导形成α-螺旋结构。

关键词: 紫外分光光度法, 多肽, 荧光分光光度法, 相互作用, 光谱法, 钙调蛋白

A deletion peptide of melittin and its analogs, Mel15, Mel15(8F) and Mel15(7P), were designed and synthesized. These peptides have very strong affinities for calmodulin, but they have short chains. Therefore they are good model peptides for the binding site of calmodulin-binding proteins. The interactions of calmodulin with them have been studied through spectral methods. The fluorescence emission spectra showed that the environment of Trp residue in Mel15 becomes more hydrophobic when Mel15 interacts with calmodulin, indicating that the Trp residue is close to the hydrophobic surface of calmodulin. The UV absorption difference spectra showed that calmodulin begins to bind Mel15(8F) after calmodulin binds 2 Ca^2^+ ions. The CD spectra showed that the binding of calmodulin with the peptides induces the increase of α-helical content. The stronger is the binding, the more residues are induced to form α-helices.

Key words: ULTRAVIOLET SPECTROPHOTOMETRY, POLYPEPTIDE, FLUOROSPECTROPHOTOMETRY, INTERACTIONS, SPECTROMETRY, CALMODULIN

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