揭示pom肽复合物：分子洞察金属氧化物纳米颗粒-蛋白质相互作用

IF 2.6 3区化学 Q2 CHEMISTRY, MULTIDISCIPLINARY

CrystEngComm Pub Date : 2025-02-25 DOI:10.1039/D4CE01269K

Björn H. Greijer and Vadim G. Kessler

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引用次数: 0

摘要

矿物纳米颗粒（NPs）在生物系统中发挥着至关重要的作用，在蛋白质氧化和水解中表现出类似酶的“纳米酶”活性。为了在分子水平上研究NP相互作用，我们表征了多肽与聚氧金属酸盐（POM）的复合物，这是已知最小的NP。我们的发现强调了诸如金属-氧键极性、肽亲水性、介质条件和结构导向氨基酸等因素的重要性。利用单晶模型和二维核磁共振，我们还探索了作为纳米酶的较大NPs与氨基酸和蛋白质特定氧化相关的蛋白质之间的相互作用。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

Unveiling POM–peptide complexes: molecular insights into metal oxide nanoparticle–protein interactions

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Unveiling POM–peptide complexes: molecular insights into metal oxide nanoparticle–protein interactions

Mineral nanoparticles (NPs) play a crucial role in biological systems, exhibiting enzyme-like “nanozyme” activity in protein oxidation and hydrolysis. To study NP interactions at the molecular level, we characterized complexes of peptides with poly-oxo-metalate (POM) species, the smallest known NPs. Our findings highlight the importance of factors such as metal–oxygen bond polarity, peptide hydrophilicity, medium conditions, and structure-directing amino acids. Using single-crystal models and 2D NMR, we also explored interactions between larger NPs as nanozymes and proteins relevant for specific oxidation of amino acids and proteins.

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