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- W2092174758 abstract "In this paper, the binding of neutral red (NR) to bovine serum albumin (BSA) under physiological conditions has been studied by spectroscopy method including fluorescence, circular dichroism (CD) and Fourier transform infrared (FT-IR) spectroscopy. The Stern–Volmer fluorescence quenching constant ( K SV ), binding constant ( K b ) and the number of binding sites ( n ) were measured by fluorescence quenching method. Fluorescence experiments were also performed at different ionic strengths. It was found K SV was ionic strength dependent, which indicated the electrostatic interactions were part of the binding forces. The distance r between donor (BSA) and acceptor (NR) was obtained according to Foster's non-radiative energy transfer theory. CD spectroscopy and FT-IR spectroscopy were used to investigate the structural information of BSA molecules on the binding of NR, and the results showed no change of BSA conformation in our experimental conditions." @default.
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- W2092174758 date "2006-11-01" @default.
- W2092174758 modified "2023-09-27" @default.
- W2092174758 title "In vitro study on the binding of neutral red to bovine serum albumin by molecular spectroscopy" @default.
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- W2092174758 doi "https://doi.org/10.1016/j.jphotochem.2006.04.003" @default.
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