Elucidation of molecular interactions between human γD-crystallin and quercetin, an inhibitor against tryptophan oxidation.

Journal of Biomolecular Structure & Dynamics
Shiwani RanaKalyan Sundar Ghosh

Abstract

Different post-translational changes in eye lens crystallin proteins contribute towards the development of cataract. We have studied in vitro oxidative modification of tryptophan (Trp) residues of human γD-crystallin (HGD) towards formation of N-formylkynurenine (NFK) associated with cataractogenesis. This oxidation was found to be inhibited by quercetin at relatively low concentration. Interactions between quercetin and HGD were further studied using fluorescence techniques. Binding and quenching constants were determined as ∼104 M-1. Static quenching of fluorescence due to HGD-quercetin complex formation at ground state was confirmed by finding excited state life time of Trp residues. Energy transfer occurred between the protein and quercetin. Hydrogen bonding and/or van der Waals interactions were involved between HGD and quercetin. Synchronous and three-dimensional fluorescence along with far-UV CD studies suggested no major conformational alterations occurred in HGD due to quercetin binding. Experimental observations were supported by the docking results.Communicated by Ramaswamy H. Sarma.

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Citations

May 30, 2020·Journal of Biomolecular Structure & Dynamics·Shiwani Rana, Kalyan Sundar Ghosh
Jun 27, 2020·Photochemical & Photobiological Sciences : Official Journal of the European Photochemistry Association and the European Society for Photobiology·Magdalena M OlchawaTadeusz J Sarna

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Methods Mentioned

BETA
circular dichroism
fluorescence spectroscopy

Software Mentioned

IBH DAS
FROG
AMMOS
Autodock

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