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Luminophore Formation in Various Conformations of Bovine Serum Albumin by Binding of Gold(III)
Published on: August 31, 2018
Studies on the interaction of colloidal gold and serum albumins by spectral methods
Dejiang Gao1, Yuan Tian, Shuyun Bi
1College of Chemistry, Jilin University, Changchun 130012, PR China.
Abstract:
The interactions of colloidal gold and serum albumins, including bovine serum albumin (BSA) and human serum albumin (HSA), were studied by fluorescence and absorption spectrometry. Fluorescence quenching spectrometry was applied to study the interactions between colloidal gold and serum albumins. At pH 7.4 phosphate-buffered saline (PBS), the intensity of fluorescence emission spectrum of serum albumins decreased in the presence of colloidal gold, which indicated that colloidal gold quenched the fluorescence of serum albumins. Experimental results indicated that the combination reactions of colloidal gold and serum albumins were static quenching processes. Based on the effect of colloidal gold on fluorescence intensity, the binding constants, the numbers of binding sites and the acting forces between colloidal gold and serum albumins were found.
