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

Chirality
Shigeru NegiY Sugiura

Abstract

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.

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Citations

Apr 12, 2008·Nucleosides, Nucleotides & Nucleic Acids·Hidehito UrataMasao Akagi
Dec 23, 2015·Analytical Chemistry·Liang CuiWeihong Tan
Feb 1, 2008·Chemistry : a European Journal·Shigeru NegiYukio Sugiura
Sep 28, 2007·Angewandte Chemie·Christian DoseChristian H Albrecht
Mar 16, 2011·Chemistry & Biodiversity·Daniele D'AlonzoGiovanni Palumbo
Mar 19, 2019·Cell Chemical Biology·Joachim WeidmannJörg D Hoheisel

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