Biomolecular mirror-image recognition: Reciprocal chiral-specific DNA binding of synthetic enantiomers of zinc finger domain from GAGA factor

被引：11

作者：

Negi, S

Dhanasekaran, M

Hirata, T

Urata, H

Sugiura, Y ^{[1
]}

机构：

[1] Doshisha Womens Univ, Fac Pharmaceut Sci, Kyotanabe 6100395, Japan

[2] Osaka Univ Pharmaceut Sci, Takatsuki, Osaka, Japan

来源：

CHIRALITY | 2006年 / 18卷 / 04期

关键词：

D-chiral peptide; DNA-recognition; GAGA factor; peptide design; transcription factor; zinc finger;

D O I：

10.1002/chir.20247

中图分类号：

R914 [药物化学];

学科分类号：

100701 ;

摘要：

To experimentally demonstrate the mirror-image recognition in protein and DNA interaction, we have designed a small DNA-binding peptide based on the zinc-finger domain of GAGA transcription factor. Circular dichroism data suggest that the conformations of peptide enantiomers as well as the DNA enantiomers have a mirror-image relationship. The gel mobility shift assay showed that the synthetic enantiomers of the peptide showed reciprocal chiral-specific interactions with the DNA; the natural L-peptide binds specifically with the natural D-DNA substrate, and the unnatural D-peptide binds specifically with the unnatural L-DNA substrate. The present data imply that the folding of the L- and D-enantiomers of the peptide as well as the DNA substrates are exact mirror images of each other in 3-D structure and biological activity, and generalize the chiral-specific nature of biomolecular interaction.

引用

页码：254 / 258

页数：5