期刊
JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY B-BIOLOGY
卷 118, 期 -, 页码 1-8出版社
ELSEVIER SCIENCE SA
DOI: 10.1016/j.jphotobiol.2012.09.010
关键词
Fluorescence; Human serum albumin; Fluorescence quenching; Thermodynamic parameters; Pyrimidine derivative
资金
- UGC, New Delhi [University Grant Commission, XIth plan (Faculty Improvement Programme)]
- DST
- UGC
Steady state fluorescence and UV-vis absorption spectroscopic techniques have been exploited to explore the binding interaction of a antibacterial pyrimidine derivative 2-amino-6-hydroxy-4-(4-hydroxy-phenyl)-pyrimidine-5-carbonitrile (AHHPPC) with the model transporter protein, human serum albumin (HSA) under the physiological conditions. It exhibits antibacterial activity against Escherichia coli and Staphylococcus aureus. Analysis of fluorescence quenching data of HSA at different temperatures using Stern-Volmer methods revealed the formation of AHHPPC-HSA complex with binding affinities of the order 10(4) M-1. The binding site number (n approximate to 1) and corresponding thermodynamic parameters (Delta G), (Delta H) and (Delta S) were calculated, indicated that binding reaction was endothermic and the hydrophobic interactions plays a major role in stabilizing the complex. The binding distance (r approximate to 3.13 nm) between donor (HSA) and acceptor (AHHPPC) was obtained according to FRET. Changes in the albumin secondary structure imparted by the compound was confirmed using synchronous fluorescence, electronic absorption, circular dichroism (CD) and three-dimensional (3D) fluorescence spectroscopy. All these experimental results clarified that AHHPPC could bind to HSA and be effectively transported and eliminated in body, which could be a useful guideline for further drug design. (C) 2012 Elsevier B.V. All rights reserved.
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