Interaction of mercury ion (Hg2+) with blood and cytotoxicity attenuation by serum albumin binding.

Blood mercury reflects the amount available from tissues, which is an indication of the exposure level. Here we confirm that Hg2+ caused hemolytic effects at high concentrations; while at light concentrations, most of the ions were bound to human serum albumin (HSA). The binding mechanism of Hg2+ to HSA has been investigated, which indicated that the presence of Hg2+ significantly perturbed the structure of HSA and quenched the fluorescence of protein in a hybrid dynamic and static mode. Hg2+ was preferably bound to cysteine and cystine, where the R‒S‒S‒R structure is responsible for maintaining the protein's structure by stabilizing the α-helical bundles. The metal-protein interaction mitigated the cellular toxicity as concealed by A498 cell lines. The fundamental and comprehensive data in this work is beneficial to elucidating and understanding the identification and binding mechanisms of heavy metals with proteins, as well as possible risks on human beings and the environment.