Department of Chemistry, KU Leuven, Celestijnenlaan 200F, 3001, Leuven, Belgium.
Angew Chem Int Ed Engl. 2023 Aug 1;62(31):e202303817. doi: 10.1002/anie.202303817. Epub 2023 May 15.
The specific interactions of anionic metal-oxo clusters, known as polyoxometalates (POMs), with proteins can be leveraged for a wide range of analytical and biomedical applications. For example, POMs have been developed as selective catalysts that can induce protein modifications and have also been shown to facilitate protein crystallization, both of which are instrumental in the structural characterization of proteins. POMs can also be used for selective protein separation and enzyme inhibition, which makes them promising therapeutic agents. Hence, understanding POM-protein interactions is essential for the development of POM-based materials and their implementation in several fields. In this Review we summarize in detail the key insights that have been gained so far on POM-protein interactions. Emphasis is also given to hybrid POMs functionalized with organic ligands to prompt further research in this direction owing to the promising recent results on tuning POM-protein interactions through POM functionalization.
阴离子金属-氧簇，即多金属氧酸盐（POMs）与蛋白质的特定相互作用可用于广泛的分析和生物医学应用。例如，POMs 已被开发为选择性催化剂，可诱导蛋白质修饰，也已被证明可促进蛋白质结晶，这两者对于蛋白质的结构特征都很重要。POMs 还可用于选择性蛋白质分离和酶抑制，这使它们成为有前途的治疗剂。因此，了解 POM-蛋白质相互作用对于基于 POM 的材料的开发及其在多个领域的应用至关重要。在这篇综述中，我们详细总结了迄今为止在 POM-蛋白质相互作用方面获得的关键见解。由于通过 POM 功能化来调节 POM-蛋白质相互作用方面的最新研究结果很有希望，因此还强调了用有机配体功能化的杂化 POMs，以促使在这一方向上进行进一步的研究。
