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Unfolding diminishes fluorescence resonance energy transfer (FRET) of lysine modified β-lactoglobulin: Relevance towards anti-HIV binding

Paper ID Volume ID Publish Year Pages File Format Full-Text
29911 44446 2011 10 PDF Available
Title
Unfolding diminishes fluorescence resonance energy transfer (FRET) of lysine modified β-lactoglobulin: Relevance towards anti-HIV binding
Abstract

In accordance with the recent reports by Ng et al. (2001) [12] and Pellengrini et al. (2001) [13], that acetylated and succinylated β-lg has a potent HIV-I and HIV-II type enzyme inhibitory activity, a spectro-fluoremetric approach has been made to understand the mode of interactions playing the key role in inhibition process. In this article, interactions between lysine modified bovine β-lactoglobulin (β-lg) and a hydrophobic fluorescence probe, 1-anilinonapthalene-8-sulfonate (ANS), have been studied with the help of fluorescence resonance energy transfer (FRET) process. Lysine residues of β-lg were modified by acetylation and succinylation. Tryptophan-19 of intact β-lg efficiently transfers energy to ANS, whereas in derivatives, it unexpectedly failed to promote energy transfer in spite of being more solvent exposed with an appreciable overlap integral. Efficient fluorescence resonance energy transfer (FRET) is a consequence of good overlap between emission and absorption spectra of donor and acceptor respectively. Therefore, linearity of this relationship becomes questionable in case of modified bio-molecules. Furthermore, time resolved studies showed that in the derivatives, hydrophobic cavities of β-lg were collapsed so that ANS failed to recognize the deep interior pockets leading to the loss of longer lifetime component. Modifications also prohibited the ionic association through surface leading to the loss of shorter lifetime component. Hence, chemical modification destabilizes β-lg conformations that affect FRET and interactions are strictly electrostatic.

Keywords
β-Lactoglobulin; Fluorescence resonance energy transfer; ANS; Lifetime decay; Acetylation; Succinylation
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Unfolding diminishes fluorescence resonance energy transfer (FRET) of lysine modified β-lactoglobulin: Relevance towards anti-HIV binding
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Photochemistry and Photobiology B: Biology - Volume 102, Issue 1, 10 January 2011, Pages 1–10
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
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