[feed] Atom [feed] RSS 1.0 [feed] RSS 2.0

Inhibition of lipoxygenase-1 by tetrahydrocurcumin.

Sneharani, A. H. and Sridevi Annapurna, Singh and Srinivas, P. and Appu Rao, A. G. (2011) Inhibition of lipoxygenase-1 by tetrahydrocurcumin. European Food Research and Technology, 233. pp. 561-568. ISSN 00217-010

[img] PDF
European_Food_Research_and_Technology_2011_233_561-568.pdf - Published Version
Restricted to Registered users only

Download (1MB) | Request a copy

Abstract

Tetrahydrocurcumin (THC)—the reduced form of curcumin—is more hydrophilic than its parent compound. It possesses higher stability in aqueous medium compared to curcumin. Lipoxygenase (LOX) enzyme is implicated in inflammatory conditions. THC was investigated for the inhibition of soy LOX-1. THC-inhibited LOX-1 with an IC50 value of 44.6 ± 0.6 lM. Kinetics of inhibition revealed mixed linear type with a Ki value of 46 lM. THC-inhibited LOX-1 by preventing the activation of LOX-1 as evidenced from spectroscopic studies. Molecular docking simulations suggested the binding of THC near the iron cofactor. This study helps in further understanding of the anti-inflammatory property of curcumin derivatives and provides valuable leads as an alternative of curcumin with better solubility and stability at physiological pH.

Item Type: Article
Uncontrolled Keywords: Tetrahydrocurcumin Lipoxygenase Redox inhibition Spectroscopic measurements
Subjects: 500 Natural Sciences and Mathematics > 07 Life Sciences > 03 Biochemistry & Molecular Biology > 18 Phytochemistry
600 Technology > 08 Food technology > 16 Nutritive value > 05 Enzymes
Divisions: Protein Chemistry and Technology
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 20 Jan 2012 07:20
Last Modified: 01 Jul 2015 11:50
URI: http://ir.cftri.com/id/eprint/10549

Actions (login required)

View Item View Item