TY - JOUR
T1 - In vitro study on the binding of neutral red to bovine serum albumin by molecular spectroscopy
AU - Shang, Li
AU - Jiang, Xiue
AU - Dong, Shaojun
PY - 2006/11/15
Y1 - 2006/11/15
N2 - 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 (KSV), binding constant (Kb) 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 KSV 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.
AB - 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 (KSV), binding constant (Kb) 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 KSV 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.
KW - Bovine serum albumin
KW - Molecular spectroscopy
KW - Neutral red
UR - http://www.scopus.com/inward/record.url?scp=33749669289&partnerID=8YFLogxK
U2 - 10.1016/j.jphotochem.2006.04.003
DO - 10.1016/j.jphotochem.2006.04.003
M3 - 文章
AN - SCOPUS:33749669289
SN - 1010-6030
VL - 184
SP - 93
EP - 97
JO - Journal of Photochemistry and Photobiology A: Chemistry
JF - Journal of Photochemistry and Photobiology A: Chemistry
IS - 1-2
ER -