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

Abstract

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; Pd^II 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.