Binding interaction of indomethacin with human serum albumin

The interaction between indomethacin and human serum albumin (HSA) was investigated by fluorescence quenching technique and UV–vis absorption spectroscopy. The results of fluorescence titration revealed that indomethacin, strongly quench the intrinsic fluorescence of HSA by static quenching and nonr...

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Bibliographic Details
Published in:Journal of pharmaceutical and biomedical analysis 2008-08, Vol.47 (4), p.981-984
Main Authors: Bogdan, M., Pirnau, A., Floare, C., Bugeac, Carmen
Format: Article
Language:English
Subjects:
Analysis
Analytical, structural and metabolic biochemistry
Anti-Inflammatory Agents, Non-Steroidal - metabolism
Binding parameters: energy transfer
Binding Sites
Biological and medical sciences
Fluorescence quenching
Fluorescence Resonance Energy Transfer - methods
Fundamental and applied biological sciences. Psychology
General pharmacology
Human serum albumin
Humans
Indomethacin
Indomethacin - metabolism
Medical sciences
Pharmacology. Drug treatments
Protein Binding
Serum Albumin - metabolism
Solutions - chemistry
Spectrophotometry, Ultraviolet - methods
Temperature
Water - chemistry
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Summary:The interaction between indomethacin and human serum albumin (HSA) was investigated by fluorescence quenching technique and UV–vis absorption spectroscopy. The results of fluorescence titration revealed that indomethacin, strongly quench the intrinsic fluorescence of HSA by static quenching and nonradiative energy transfer. The binding site number n and the apparent binding constant K A, were calculated using linear and nonlinear fit to the experimental data. The distance r between donor (HSA) and acceptor (indomethacin) was obtained according to fluorescence resonance energy transfer (FRET). The study suggests that the donor and the acceptor are bound at different locations but within the quenching distance.
ISSN:0731-7085
1873-264X
DOI:10.1016/j.jpba.2008.04.003