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

Shanjun Song, Yiling Li, Qian S. Liu, Huiyu Wang, Penghui Li, Jianbo Shi, Ligang Hu, Haiyan Zhang, Yuanchen Liu, Kun Li, Xingchen Zhao*, Zongwei Cai*

*Corresponding author for this work

Research output: Contribution to journalJournal articlepeer-review

27 Citations (Scopus)


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.

Original languageEnglish
Article number125158
JournalJournal of Hazardous Materials
Early online date23 Jan 2021
Publication statusPublished - 15 Jun 2021

Scopus Subject Areas

  • Environmental Engineering
  • Environmental Chemistry
  • Waste Management and Disposal
  • Pollution
  • Health, Toxicology and Mutagenesis

User-Defined Keywords

  • Binding mechanism
  • Mercury
  • Plasma
  • Protein identification
  • Reduced toxicity


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