Journal
JOURNAL OF LUMINESCENCE
Volume 129, Issue 1, Pages 34-39Publisher
ELSEVIER
DOI: 10.1016/j.jlumin.2008.07.012
Keywords
Energy transfer; Binding parameter; Thermodynamic parameter; Laser flash photolysis; Bovine serum albumin; Proflavin
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The interaction of bovine serum albumin (BSA) with proflavin was investigated by spectroscopic tools like absorption and fluorescence spectroscopy as well as laser flash photolysis. Absorption spectroscopy proved the formation of ground-state BSA-proflavin complex. Proflavin was found to quench the intrinsic fluorescence of BSA via static quenching. High value of quenching constant suggested that energy transfer occurred from BSA to proflavin. Distance between the fluorophore in the protein and the ligand (proflavin) was evaluated. Binding constant and number of binding site were determined for proflavin-BSA interaction both in phosphate buffer (pH similar to 6.8) and in sodium dodecylsulphate media. The values of the thermodynamic parameters suggested that the key interacting forces are van der Waal's interaction and hydrogen bonding. Laser flash photolysis study reconfirmed the formation of complex between BSA and proflavin. (C) 2008 Elsevier B.V. All rights reserved.
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