| Literature DB >> 21416257 |
Jayaraman Jayabharathi1, Venugopal Thanikachalam, Marimuthu Venkatesh Perumal, Kanagarathinam Saravanan.
Abstract
The mutual interaction of imidazole derivative (PIPP) with bovine serum albumin (BSA) was investigated using photoluminescent studies. The fluorescence quenching mechanism of BSA by PIPP was analyzed and the binding constant was calculated. The binding distance between PIPP and BSA was obtained based on the theory of Forester's non-radiation energy transfer. Displacement experiments were performed by using ibuprofen to identify PIPP binding site in BSA. The effect of some common ions on the binding constant between PIPP and BSA was also examined. © Springer Science+Business Media, LLC 2011Entities:
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Year: 2011 PMID: 21416257 DOI: 10.1007/s10895-011-0878-3
Source DB: PubMed Journal: J Fluoresc ISSN: 1053-0509 Impact factor: 2.217