CLC number: O657.3
On-line Access: 2024-08-27
Received: 2023-10-17
Revision Accepted: 2024-05-08
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FAN Ji-cai, CHEN Xiang, WANG Yun, FAN Cheng-ping, SHANG Zhi-cai. Binding interactions of pefloxacin mesylate with bovine lactoferrin and human serum albumin[J]. Journal of Zhejiang University Science B, 2006, 7(6): 452-458.
@article{title="Binding interactions of pefloxacin mesylate with bovine lactoferrin and human serum albumin",
author="FAN Ji-cai, CHEN Xiang, WANG Yun, FAN Cheng-ping, SHANG Zhi-cai",
journal="Journal of Zhejiang University Science B",
volume="7",
number="6",
pages="452-458",
year="2006",
publisher="Zhejiang University Press & Springer",
doi="10.1631/jzus.2006.B0452"
}
%0 Journal Article
%T Binding interactions of pefloxacin mesylate with bovine lactoferrin and human serum albumin
%A FAN Ji-cai
%A CHEN Xiang
%A WANG Yun
%A FAN Cheng-ping
%A SHANG Zhi-cai
%J Journal of Zhejiang University SCIENCE B
%V 7
%N 6
%P 452-458
%@ 1673-1581
%D 2006
%I Zhejiang University Press & Springer
%DOI 10.1631/jzus.2006.B0452
TY - JOUR
T1 - Binding interactions of pefloxacin mesylate with bovine lactoferrin and human serum albumin
A1 - FAN Ji-cai
A1 - CHEN Xiang
A1 - WANG Yun
A1 - FAN Cheng-ping
A1 - SHANG Zhi-cai
J0 - Journal of Zhejiang University Science B
VL - 7
IS - 6
SP - 452
EP - 458
%@ 1673-1581
Y1 - 2006
PB - Zhejiang University Press & Springer
ER -
DOI - 10.1631/jzus.2006.B0452
Abstract: The binding of pefloxacin mesylate (PFLX) to bovine lactoferrin (BLf) and human serum albumin (HSA) in dilute aqueous solution was studied using fluorescence spectra and absorbance spectra. The binding constant K and the binding sites n were obtained by fluorescence quenching method. The binding distance r and energy-transfer efficiency E between pefloxacin mesylate and bovine lactoferrin as well as human serum albumin were also obtained according to the mechanism of Förster-type dipole-dipole nonradiative energy-transfer. The effects of pefloxacin mesylate on the conformations of bovine lactoferrin and human serum albumin were also analyzed using synchronous fluorescence spectroscopy.
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