Front Cover: Exploiting SpyTag/SpyCatcher Technology to Design New Artificial Catalytic Copper Proteins (ChemBioChem 14/2025)

IF 2.8 4区 生物学 Q3 BIOCHEMISTRY & MOLECULAR BIOLOGY
ChemBioChem Pub Date : 2025-07-21 DOI:10.1002/cbic.202581401
Silvia Gentili, Francesca Miglioli, Valentina Borghesani, Gloria Spagnoli, Denise Bellotti, Davide Cavazzini, Remo Guerrini, Maurizio Remelli, Giovanni Maestri, Simone Ottonello, Angelo Bolchi, Matteo Tegoni
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引用次数: 0

Abstract

Designing artificial metal sites in proteins is challenging due to the need to place the metal site in precise positions and to tailor the coordination environment of the metal. In article 10.1002/cbic.202500208, Matteo Tegoni and co-workers use a modular approach using the SpyTag/SpyCatcher technology to provide the Spy construct with a Cu2+/ATCUN site. The reconstituted copper protein showed enhanced ROS catalytic activity. This strategy enables versatile metalloprotein design by shifting complexity from a protein to a peptide.

Abstract Image

封面:利用SpyTag/SpyCatcher技术设计新型人工催化铜蛋白(ChemBioChem 14/2025)
在蛋白质中设计人工金属位点是具有挑战性的,因为需要将金属位点放置在精确的位置并定制金属的协调环境。见第10.1002/ cic条。202500208, Matteo Tegoni及其同事使用SpyTag/SpyCatcher技术的模块化方法为Spy结构提供Cu2+/ATCUN位点。重组铜蛋白对活性氧的催化活性增强。该策略通过将复杂性从蛋白质转移到肽,使多功能金属蛋白设计成为可能。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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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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