Interactions of Aromatic Residues in Amyloids: A Survey of Protein Data Bank Crystallographic Data,Crystal Growth & Design

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Interactions of Aromatic Residues in Amyloids: A Survey of Protein Data Bank Crystallographic Data
Crystal Growth & Design ( IF 3.2 ) Pub Date : 2017-11-09 00:00:00 , DOI: 10.1021/acs.cgd.7b01035
Ivana M. Stanković ₁ , Dragana M. Božinovski ₂ , Edward N. Brothers ₃ , Milivoj R. Belić ₃ , Michael B. Hall ₄ , Snežana D. Zarić _{2,

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Affiliation

Aromatic–aromatic interactions have long been considered important in the self-assembly of amyloids. In spite of their importance, aromatic amino acids are not detected in every amyloid. In the present study, the occurrence and geometry of these interactions were analyzed for the amyloid structures found in the Protein Data Bank. The data confirm that aromatic amino acids are not crucial for amyloid fibril formation. In fact, aromatic–aliphatic interactions are more frequent than the aromatic–aromatic interactions. Aromatic–aliphatic interactions are present in higher numbers of structures and in certain amyloid sequences they are more frequent than aromatic–aromatic interactions. An analysis of aromatic/aromatic interactions shows different interaction geometries in intrasheet and intersheet contacts; the intrasheet aromatic–aromatic interactions are mostly parallel and displaced, while intersheet interactions are not parallel. Thus, among the aromatic–aromatic interactions there are important edge-to-face attractions in addition to parallel stacking ones.

中文翻译：

淀粉样蛋白中的芳香残基的相互作用：蛋白质数据库晶体学数据的调查。

长期以来，芳香-芳香相互作用一直被认为在淀粉样蛋白的自组装中很重要。尽管它们很重要，但并非在每个淀粉样蛋白中都检测到芳香族氨基酸。在本研究中，针对蛋白质数据库中发现的淀粉样蛋白结构分析了这些相互作用的发生和几何形状。数据证实，芳香族氨基酸对于淀粉样蛋白原纤维的形成不是至关重要的。实际上，芳族-脂族的相互作用比芳族-芳族的相互作用更为频繁。芳香-脂肪相互作用以较高数量的结构存在，并且在某些淀粉样序列中，它们比芳香-芳香相互作用更频繁。对芳族/芳族相互作用的分析显示，片内和片间接触具有不同的相互作用几何形状。片内的芳香-芳族相互作用大部分是平行和位移的，而片间的相互作用则不平行。因此，在芳香-芳香相互作用中，除了平行堆积外，还有重要的边对边吸引。

更新日期：2017-11-09

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