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Updated: Oct 14, 2025

Luminophore Formation in Various Conformations of Bovine Serum Albumin by Binding of GoldIII
Published on: August 31, 2018
Investigation on the interaction between Ag+ and bovine hemoglobin using spectroscopic methods
Zhenxing Chi1, Ling Weng1, Xunuo Zhang1
1School of Marine Science and Technology, Harbin Institute of Technology, Weihai, Weihai, PR China.
Abstract:
Silver ions (Ag+) can be released by silver nanoparticles (AgNPs) which are widely used in diverse fields. Ag+ can exist inside cells to produce cytotoxicity. This report uses spectroscopic methods to reveal the interactions between Ag+ and bovine hemoglobin (BHb). The results of the quenching rate constant (Kq) and the fluorescence lifetime detection showed that the quenching mechanism of BHb by Ag+ was static. Thermodynamic investigations indicated that Ag+ can interact with BHb with one binding site to form complex mainly through van der Waals interactions and hydrogen bonds. The UV-vis absorption and synchronous fluorescence spectra showed that Ag+ changed the conformation of BHb, which may affect protein functions. This research is favorable for understanding the molecular toxic mechanism of Ag+ in vivo.
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