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Luminophore Formation in Various Conformations of Bovine Serum Albumin by Binding of GoldIII
Published on: August 31, 2018
Investigation on the interaction of pyrene with bovine serum albumin using spectroscopic methods
Chengbin Xu1, Jiali Gu2, Xiping Ma1
1School of Environmental Science, Liaoning University, Shenyang 110036, China.
Abstract:
This paper was designed to investigate the interaction of pyrene with bovine serum albumin (BSA) under physiological condition by spectroscopic methods. Spectroscopic analysis of the emission quenching revealed that the quenching mechanism of BSA by pyrene was static. The binding sites and constants of pyrene-BSA complex were observed to be 1.20 and 2.63×10(6) L mol(-1) at 298 K, respectively. The enthalpy change (ΔH) and entropy change (ΔS) revealed that van der Waals forces and hydrogen bonds stabilized the pyrene-BSA complex. Energy transfer from tryptophan to pyrene occurred by a FRET (fluorescence resonance energy transfer) mechanism, and the distance (r=2.72 nm) had been determined. The results of synchronous, three-dimensional fluorescence, and circular dichroism spectra showed that the pyrene induced conformational changes of BSA.
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