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含有表面活性剂胶束的水溶液中反向蜂毒素 I 的构象

Conformation of retro-bombolitin I in aqueous solution containing surfactant micelles.

作者信息

Battistutta R, Bisello A, Mammi S, Peggion E

机构信息

Department of Organic Chemistry, University of Padua, Italy.

出版信息

Biopolymers. 1994 Nov;34(11):1535-41. doi: 10.1002/bip.360341111.

Abstract

Bombolitins are five naturally occurring heptadecapeptides acting at the membrane level and able to increase the activity of phospholipase A2. As for other peptides with similar function, the biological activity of bombolitins seems to be mainly due to their ability to form amphipathic helical structures. We synthesized and tested the retro sequence of bombolitin I (retro-bombolitin I). This peptide showed an activity similar to that of the natural sequence and was able to adopt a helical structure in the presence of an amphipathic environment consisting of SDS micelles. The secondary structure of this peptide was fully characterized by CD and nmr spectroscopy.

摘要

蜂毒素是五种天然存在的十七肽,作用于膜水平,能够增加磷脂酶A2的活性。与其他具有类似功能的肽一样,蜂毒素的生物活性似乎主要归因于它们形成两亲性螺旋结构的能力。我们合成并测试了蜂毒素I的反向序列(反向蜂毒素I)。该肽表现出与天然序列相似的活性,并且在由SDS胶束组成的两亲性环境中能够形成螺旋结构。通过圆二色光谱和核磁共振光谱对该肽的二级结构进行了全面表征。

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