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Study of interaction of proton transfer probe 1-hydroxy-2-naphthaldehyde with serum albumins: A spectroscopic study

Paper ID Volume ID Publish Year Pages File Format Full-Text
31140 44554 2008 8 PDF Available
Title
Study of interaction of proton transfer probe 1-hydroxy-2-naphthaldehyde with serum albumins: A spectroscopic study
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 (ΔG) 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.

Keywords
1-Hydroxy-2-naphthaldehyde; Serum albumins; Absorption; Fluorescence emission; Fluorescence resonance energy transfer
First Page Preview
Study of interaction of proton transfer probe 1-hydroxy-2-naphthaldehyde with serum albumins: A spectroscopic study
Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Photochemistry and Photobiology B: Biology - Volume 91, Issue 1, 25 April 2008, Pages 1–8
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering