Surewicz W K, Mantsch H H, Stahl G L, Epand R M
Division of Chemistry, National Research Council of Canada, Ottawa, ON.
Proc Natl Acad Sci U S A. 1987 Oct;84(20):7028-30. doi: 10.1073/pnas.84.20.7028.
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.
通过傅里叶变换红外光谱法研究了心房利钠肽心钠素III的构象性质。使用去卷积和谱带拟合程序对酰胺I区域的红外光谱进行了定量分析。根据该分析，在水溶液中单体肽具有无规结构。与二肉豆蔻酰磷脂酰甘油双层囊泡结合会导致剧烈的构象变化。脂质复合的心钠素III采用主要为β-折叠的高度有序结构。肽自缔合时会发生向相似但不完全相同的β-结构的转变。模型实验结果表明，这种心房肽与靶细胞膜的结合与β-折叠结构的诱导有关，并且正是这种后者的构象在激素的活性形式中占主导地位。
