Investigation on the interaction of prulifloxacin with human serum albumin: a spectroscopic analysis.
The interaction between prulifloxacin (PUFX) and human serum albumin (HSA) was investigated under simulated physiologic conditions with fluorescence spectra. The fluorescence quenching process of HSA may be mainly governed by a static quenching mechanism. The apparent binding constant K(b) between PUFX and HSA at different temperatures were 2.08+/-1.04, 2.74+/-0.50, and 4.98+/-1.61x10(8) l/mol. The thermodynamic parameters, with a negative value of DeltaG(0), revealed that the binding is a spontaneous process. A binding distance R of 1.19 nm between donor and acceptor was obtained from the Fŏrster energy transfer theory.
Huang
Ya-Bei
YB
Department of Chemistry, Huaibei Coal Normal College, Huaibei Occupational Disease Prevention and Cure Hospital, Huaibei, Anhui Province, P R China
Wang
Shi-Jun
SJ
Zi
Yan-Qin
YQ
Yu
Zhang
Z
Gao
Xiao-Yan
XY
Tang
Ying-Cai
YC
Zhang
Da-Ming
DM
D001665:Binding Sites; D004148:Dioxolanes / Q000737:chemistry / Q000378:metabolism*; D024841:Fluoroquinolones / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D010879:Piperazines / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D012709:Serum Albumin / Q000737:chemistry / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D013816:Thermodynamics
D004148:Dioxolanes; D024841:Fluoroquinolones; D010879:Piperazines; D012709:Serum Albumin; C074191:prulifloxacin