Position-Regulated Electrostatic Interactions for Single Amino Acid Revealed by Aspartic Acid-Scanning Mutagenesis.

IF 2.6 4区 生物学 Q3 BIOCHEMISTRY & MOLECULAR BIOLOGY
ChemBioChem Pub Date : 2024-12-12 DOI:10.1002/cbic.202400891
Mengting Chen, Lilusi Ma, Minxian Li, Xiaocui Fang, Yanlian Yang, Chen Wang
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引用次数: 0

Abstract

We have examined in this contribution the electrostatic interactions between single arginine and aspartic acid by analyzing the peptide-peptide binding characteristics involving arginine-aspartic acid, arginine-glycine, arginine-tryptophan and tryptophan-glycine interactions. The results of aspartic acid mutagenesis revealed that the interactions between arginine and aspartic acid have significant dependence on the position and composition of amino acids. While the primary interaction can be attributed to arginine-tryptophan contacts originated from the indole moieties with the main chains of 14-mers containing N-H and C=O moieties, pronounced enhancement could be identified in association with the electrostatic side-chain-side-chain interactions between arginine and aspartic acid. An optimal separation of 2~4 amino acids between two adjacent aspartic acid and tryptophan binding sites can be identified to achieve maximal enhancement of binding interactions. Such observed separation dependence may be utilized to unravel cooperative effects in heterogeneous interactions between single pair of amino acids.

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来源期刊
ChemBioChem
ChemBioChem 生物-生化与分子生物学
CiteScore
6.10
自引率
3.10%
发文量
407
审稿时长
1 months
期刊介绍: ChemBioChem (Impact Factor 2018: 2.641) publishes important breakthroughs across all areas at the interface of chemistry and biology, including the fields of chemical biology, bioorganic chemistry, bioinorganic chemistry, synthetic biology, biocatalysis, bionanotechnology, and biomaterials. It is published on behalf of Chemistry Europe, an association of 16 European chemical societies, and supported by the Asian Chemical Editorial Society (ACES).
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