Infrared spectroscopic evidence of conformational transitions of an atrial natriuretic peptide.
Infrared spectroscopic evidence of conformational transitions of an atrial natriuretic peptide.
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DOI：
10.1073/pnas.84.20.7028
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发表时间：
1987-10
影响因子：
11.1
通讯作者：
W. Surewicz;H. Mantsch;G. L. Stahl;R. Epand
中科院分区：
文献类型：
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作者：
W. Surewicz;H. Mantsch;G. L. Stahl;R. Epand
采用傅里叶变换红外光谱研究了心房利钠肽心房肽肽III的构象性质。利用反褶积和带拟合程序定量分析了酰胺I区的红外光谱。根据这一分析，在水溶液中，单体肽具有随机结构。与二肉豆蔻酰磷脂酰甘油的双层囊泡结合会导致剧烈的构象变化。脂质络合atriopeptin III采用高度有序的结构，主要是β -片。过渡到一个类似的，但不完全相同的，β结构发生在肽的自结合。模型实验的结果表明，心房肽与靶细胞膜的结合与β -片结构的诱导有关，而这种结构在激素的活性形式中占主导地位。
The conformational properties of the atrial natriuretic peptide atriopeptin III were investigated by Fourier-transform infrared spectroscopy. Infrared spectra in the amide I region were analyzed quantitatively using deconvolution and band-fitting procedures. According to this analysis, in aqueous solution the monomeric peptide has a random structure. Binding to bilayer vesicles of dimyristoyl phosphatidylglycerol results in drastic conformational changes. The lipid-complexed atriopeptin III adopts a highly ordered structure of predominantly beta-sheets. A transition to a similar, but not identical, beta-structure occurs upon self-association of the peptide. The results of model experiments suggest that the binding of this atrial peptide to the target cell membrane is associated with the induction of beta-sheet structure and that it is this latter conformation that is predominant in the active form of the hormone.