Interaction of bisphenol A 3, 4-quinone metabolite with human hemoglobin, human serum albumin and cytochrome c in vitro

Qian Wu, Hongzhi Zhao, Xiangfeng Chen, Zongwei CAI*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

4 Citations (Scopus)

Abstract

Since covalent protein-bisphenol A adducts generated by the interaction of protein nucleophiles with bisphenol A quinone affect the physicochemical properties of proteins in functional foods and biological tissues, it has become a hot topic nowadays. Therefore, we investigated the interaction of several different biomacromolecules such as hemoglobin, human serum albumin and cytochrome c with bisphenol A 3, 4-quinone (BPAQ). The effects of binding on changes in biomolecular structure were determined by various spectroscopic methods. BPAQ effects were investigated by using the UV–Vis spectroscopy and the quenching phenomenon from fluorescence emission. It proved that the formation of bio-complex and their aromatic micro-environment was likely to be disturbed with as well. Changes observed in circular dichroism (CD) spectroscopy confirmed the quantitative loss of the alpha-helical structure. Further studies with matrix-assisted laser desorption/ionization-time of flight mass spectrometry (MALDI-TOFMS) and molecular docking indicated combining ratio and binding sites between proteins and BPAQ. The in vitro data of BPAQ-proteins adducts may provide a valuable theoretical basis for the elucidation of the toxicological mechanisms of BPAQ adducts in biological systems and environments.

Original languageEnglish
Pages (from-to)930-936
Number of pages7
JournalChemosphere
Volume220
DOIs
Publication statusPublished - Apr 2019

Scopus Subject Areas

  • Environmental Engineering
  • Environmental Chemistry
  • Chemistry(all)
  • Pollution
  • Health, Toxicology and Mutagenesis

User-Defined Keywords

  • Bisphenol A
  • Bisphenol A 3,4-quinone
  • Cytochrome c
  • Hemoglobin
  • Human serum albumin

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