A pair of pyrene groups as a conformational probe for antiparallel beta-sheet structure, formed in cyclic peptides

被引：22

作者：

Mihara, H ^{[1
]}

Hayashida, J ^{[1
]}

Hasegawa, H ^{[1
]}

Ogawa, HI ^{[1
]}

Fujimoto, T ^{[1
]}

Nishino, N ^{[1
]}

机构：

[1] KYUSHU INST TECHNOL,FAC ENGN,DEPT APPL CHEM,KITAKYUSHU,FUKUOKA 804,JAPAN

来源：

JOURNAL OF THE CHEMICAL SOCIETY-PERKIN TRANSACTIONS 2 | 1997年 / 03期

关键词：

D O I：

10.1039/a606247d

中图分类号：

O62 [有机化学];

学科分类号：

070303 ; 081704 ;

摘要：

We have developed the utility of a pair of pyrene groups on L-1-pyrenylalanines (Pya) as a conformational probe for designed,peptides composed of alpha-helices. Here we expand the usefulness of the probing method to the antiparallel beta-sheet structure formed in cyclic peptides. A pair of Pya residues were introduced into cyclic decapeptides, gramicidin S and its analogous peptide, at various positions which were involved in antiparallel beta-sheet structures with amphiphilic character. When the two Pya residues were deployed on different beta-strands, exciton interaction in circular dichroism spectra showed that the two pyrene rings were arranged with a left-handed twist. They were orientated in a right-handed sense in the same strand. The pyrene rings showed strong excimer emission; These results demonstrate that the behaviour of the pyrene probe is coincident with the left-handed orientation of two beta-strands and the right-handed twist of a single beta-strand in natural protein structures.

引用

页码：517 / 522

页数：6

共 74 条

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