Influence of Cd2+, Hg2+ and Pb2+ on (+)-catechin binding to bovine serum albumin studied by fluorescence spectroscopic methods

The effect of heavy metal ions, Cd2+, Hg2+ and Pb2+ on (+)-catechin binding to bovine serum albumin (BSA) has been investigated by spectroscopic methods. The results indicated that the presence of heavy metal ions significantly affected the binding modes and binding affinities of (+)-catechin to BSA, and the effects depend on the types of heavy metal ion. One binding mode was found for (+)-catechin with and without Cd2+, while two binding modes – a weaker one at low concentration and a stronger one at high concentration were found for (+)-catechin in the presence of Hg2+ and Pb2+. The presence of Cd2+ decreased the binding affinities of (+)-catechin for BSA by 20.5%. The presence of Hg2+ and Pb2+ decreased the binding affinity of (+)-catechin for BSA by 8.9% and 26.7% in lower concentration, respectively, and increased the binding affinity of (+)-catechin for BSA by 5.2% and 9.2% in higher concentration, respectively. The changed binding affinity and binding distance of (+)-catechin for BSA in the presence of Cd2+, Hg2+ and Pb2+ were mainly because of the conformational change of BSA induced by heavy metal ions. However, the quenching mechanism for (+)-catechin to BSA was based on static quenching combined with non-radiative energy transfer irrespective of the absence or presence of heavy metal ions.

The presence of toxic heavy metal ions significantly affected the binding modes and binding affinities of (+)-catechin to BSA, and the effects depended on the types of metal ions.Figure optionsDownload as PowerPoint slideHighlights
► Effect of heavy metal ions on (+)-catechin binding with BSA has been studied.
► Binding affinities and binding modes of (+)-catechin to BSA have been changed.
► Conformational change was the main factor to change the binding affinity.
► The results were related to the toxic ions/drug interference.