真菌代谢产物。XX。脯氨酸残基对形成离子通道的肽——毛孢子菌素B-VIa结构的影响。

Fungal metabolites. XX. Effect of proline residue on the structure of ion-channel-forming peptide, trichosporin B-VIa.

作者信息

Nagaoka Y, Iida A, Tachikawa E, Fujita T

机构信息

Faculty of Pharmaceutical Sciences, Kyoto University, Japan.

出版信息

Chem Pharm Bull (Tokyo). 1995 Jul;43(7):1119-24. doi: 10.1248/cpb.43.1119.

DOI:10.1248/cpb.43.1119

PMID:7586054

Abstract

The secondary structures of an ion-channel-forming icosapeptaibol, trichosporin B-VIa, and its Aib14-substituted derivative containing no Pro were investigated on the basis of CD and various NM experiments in methanol. Trichosporin B-VIa has a fully helical structure with a kink stabilized by a 1<--4 hydrogen-bond between the Leu12 CO and Val15 NH. The helical structure is composed of 3(10)-helix in the N-terminal first turn and the C-terminal moiety following Leu12, and alpha-helix in the middle region. In contrast, the Aib14 derivative predominantly has a straight alpha-helical structure except for a 3(10)-helix region in the N-terminal first turn.

摘要

基于圆二色光谱（CD）和甲醇中各种核磁共振（NM）实验，对一种形成离子通道的二十肽抗生素trichosporin B-VIa及其不含脯氨酸的Aib14取代衍生物的二级结构进行了研究。Trichosporin B-VIa具有完全螺旋结构，在Leu12羰基（CO）和Val15氨基（NH）之间通过1<--4氢键稳定存在一个扭结。螺旋结构由N端第一圈的3(10)-螺旋和Leu12之后的C端部分以及中间区域的α-螺旋组成。相比之下，Aib14衍生物除了N端第一圈的3(10)-螺旋区域外，主要具有直的α-螺旋结构。