封面:NiII、PdII和PtII吡咯亚胺螯合物与人血清白蛋白相互作用的络合作用(ChemistryEurope2/2023)

Sheldon Sookai, Prof. Dr. Orde Q. Munro
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引用次数: 0

摘要

封面描绘了人血清白蛋白(HSA,蓝绿色线圈)在多个结合位点(紫色空间填充模型;PdII螯合物物种)结合几种中性、二价的第10族金属螯合物。自发金属螯合物/配体吸收的热力学由金属离子的身份决定。虽然反应是焓驱动的,但随着金属离子尺寸的增加,熵的贡献变得更加有利。重要的是,螯合物在被HSA吸收时不会脱金属,Sheldon Sookai和Orde详细介绍了这一点 Q.Munro在他们的研究文章中。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

Front Cover: Complexities of the Interaction of NiII, PdII and PtII Pyrrole-Imine Chelates with Human Serum Albumin (ChemistryEurope 2/2023)

Front Cover: Complexities of the Interaction of NiII, PdII and PtII Pyrrole-Imine Chelates with Human Serum Albumin (ChemistryEurope 2/2023)

The Front Cover depicts binding of several neutral, divalent Group 10 metal chelates by human serum albumin (HSA, teal coils) at multiple binding sites (purple space-filling models; PdII chelate species). The thermodynamics of spontaneous metal chelate/ligand uptake are governed by the identity of the metal ion. While the reactions are enthalpically driven, the entropy contribution becomes more favourable with increasing metal ion size. Importantly, the chelates do not demetallate upon uptake by HSA, as detailed by Sheldon Sookai and Orde Q. Munro in their Research Article.

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