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
收藏
页码:517 / 522
页数:6
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