Wang Sujing, Ly Hong Giang T, Wahiduzzaman Mohammad, Simms Charlotte, Dovgaliuk Iurii, Tissot Antoine, Maurin Guillaume, Parac-Vogt Tatjana N, Serre Christian
Institut des Matériaux Poreux de Paris, Ecole Normale Supérieure, ESPCI Paris, CNRS, PSL Université, Paris, France.
CAS Key Laboratory of Microscale Magnetic Resonance and Suzhou Institute for Advanced Research, University of Science and Technology of China, Hefei, China.
Nat Commun. 2022 Mar 11;13(1):1284. doi: 10.1038/s41467-022-28886-5.
The discovery of nanozymes for selective fragmentation of proteins would boost the emerging areas of modern proteomics, however, the development of efficient and reusable artificial catalysts for peptide bond hydrolysis is challenging. Here we report the catalytic properties of a zirconium metal-organic framework, MIP-201, in promoting peptide bond hydrolysis in a simple dipeptide, as well as in horse-heart myoglobin (Mb) protein that consists of 153 amino acids. We demonstrate that MIP-201 features excellent catalytic activity and selectivity, good tolerance toward reaction conditions covering a wide range of pH values, and importantly, exceptional recycling ability associated with easy regeneration process. Taking into account the catalytic performance of MIP-201 and its other advantages such as 6-connected Zr cluster active sites, the green, scalable and cost-effective synthesis, and good chemical and architectural stability, our findings suggest that MIP-201 may be a promising and practical alternative to commercially available catalysts for peptide bond hydrolysis.
发现用于蛋白质选择性片段化的纳米酶将推动现代蛋白质组学新兴领域的发展，然而，开发高效且可重复使用的肽键水解人工催化剂具有挑战性。在此，我们报告了一种锆基金属有机框架MIP-201在促进简单二肽以及由153个氨基酸组成的马心肌红蛋白（Mb）蛋白质中的肽键水解方面的催化特性。我们证明，MIP-201具有出色的催化活性和选择性，对涵盖广泛pH值范围的反应条件具有良好的耐受性，重要的是，具有与易于再生过程相关的出色循环利用能力。考虑到MIP-201的催化性能及其其他优点，如六连接的Zr簇活性位点、绿色、可扩展且具有成本效益的合成以及良好的化学和结构稳定性，我们的研究结果表明，MIP-201可能是用于肽键水解的商业可用催化剂的一种有前途且实用的替代品。
