| Literature DB >> 18296059 |
Rupashree Balia Singh1, Subrata Mahanta, Nikhil Guchhait.
Abstract
In the present work, we have studied the interaction of proton transfer probe 1-hydroxy-2-naphthaldehyde (HN12) with Human Serum Albumin (HSA) and Bovine Serum Albumin (BSA) by steady state absorption and emission spectroscopy combined with time resolved fluorescence measurements. The measured binding constant (K) and free energy change (DeltaG) indicate a stronger affinity of HN12 molecule for HSA than BSA. Steady state anisotropy, excitation anisotropy and fluorescence resonance energy transfer (FRET) studies indicate that the probe molecule resides at the hydrophobic site of the protein environment.Entities:
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Year: 2008 PMID： 18296059 DOI： 10.1016/j.jphotobiol.2007.12.006
Source DB: PubMed Journal: J Photochem Photobiol B ISSN： 1011-1344 Impact factor: 6.252