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 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.
Bogdan
M
M
National Institute for Research and Development of Isotopic and Molecular Technologies, P.O. Box 700, 400293 Cluj-Napoca, Romania. mircea@s3.itim-cj.ro
Pirnau
A
A
Floare
C
C
Bugeac
Carmen
C
D000894:Anti-Inflammatory Agents, Non-Steroidal / Q000378:metabolism*; D001665:Binding Sites; D031541:Fluorescence Resonance Energy Transfer / Q000379:methods*; D006801:Humans; D007213:Indomethacin / Q000378:metabolism*; D011485:Protein Binding; D012709:Serum Albumin / Q000378:metabolism*; D012996:Solutions / Q000737:chemistry; D013056:Spectrophotometry, Ultraviolet / Q000379:methods*; D013696:Temperature; D014867:Water / Q000737:chemistry
D000894:Anti-Inflammatory Agents, Non-Steroidal; D012709:Serum Albumin; D012996:Solutions; D014867:Water; D007213:Indomethacin