Structural and biochemical characterisation of Co²⁺-binding sites on serum albumins and their interplay with fatty acids.

ABSTRACT: Serum albumin-Co²⁺ interactions are of clinical importance. They play a role in mediating the physiological effects associated with cobalt toxicity and are central to the albumin cobalt binding (ACB) assay for diagnosis of myocardial ischemia. To further understand these processes, a deeper understanding of albumin-Co²⁺ interactions is required. Here, we present the first crystallographic structures of human serum albumin (HSA; three structures) and equine serum albumin (ESA; one structure) in complex with Co²⁺. Amongst a total of sixteen sites bearing a cobalt ion across the structures, two locations were prominent, and they relate to metal-binding sites A and B. Site-directed mutagenesis and isothermal titration calorimetry (ITC) were employed to characte

SUBMITTER: Wu D 

PROVIDER: S-EPMC10266443 | biostudies-literature | 2023 Jun

REPOSITORIES: biostudies-literature