Inhibitory effect of apocarotenoids on the activity of tyrosinase: Multi-spectroscopic and docking studies.

Abstract

In this present study, the inhibitory mechanism of three selected apocarotenoids (bixin, norbixin and crocin) on the diphenolase activity of tyrosinase has been investigated. The preliminary screening results indicated that apocarotenoids inhibited tyrosinase activity in a dose-dependent manner. Kinetic analysis revealed that apocarotenoids reversibly inhibited tyrosinase activity. Analysis of fluorescence spectra showed that apocarotenoids quenched the intrinsic fluorescence intensity of the tyrosinase. Further, molecular docking results implied that apocarotenoids were allosterically bound to tyrosinase through hydrophobic interactions. The results of the in vitro studies suggested that higher concentrations of bixin and norbixin inhibited tyrosinase activity in B16F0 melanoma cells. Our results suggested that apocarotenoids could form the basis for the design of novel tyrosinase inhibitors.

• Authors: Amrita Anantharaman, Hridya Hemachandran, Rajendra Rao Priya, Mohan Sankari, Mohan Gopalakrishnan, Nallasamy Palanisami, Ramamoorthy Siva
• Journal: Journal of bioscience and bioengineering (J Biosci Bioeng) Vol. 121 Issue 1 Pg. 13-20 (Jan 2016) ISSN: 1347-4421 [Electronic] Japan
• PMID: 26187443 (Publication Type: Journal Article)
• Copyright: Copyright © 2015 The Society for Biotechnology, Japan. Published by Elsevier B.V. All rights reserved.

Chemical References

• Melanins
• Carotenoids
• crocin
• bixin
• norbixin
• Monophenol Monooxygenase

Topics

• Allosteric Site
• Animals
• Carotenoids (pharmacology)
• Cell Line, Tumor
• Dose-Response Relationship, Drug
• Hydrophobic and Hydrophilic Interactions
• Kinetics
• Melanins (biosynthesis)
• Melanoma (enzymology)
• Mice
• Molecular Docking Simulation
• Monophenol Monooxygenase (antagonists & inhibitors, metabolism)
• Protein Binding
• Spectrometry, Fluorescence