title: Inhibitory effect of brazilein on tyrosinase and melanin synthesis: Kinetics and in silico approach.
abstract: In our present study, the inhibitory effect of brazilein from Caesalpinia sappan on tyrosinase activity was investigated through multi-spectroscopic and molecular docking techniques. The result has shown that brazilein reversibly inhibited tyrosinase in a mixed type manner. The interaction of brazilein with the amino acid residues of tyrosinase has been validated through fluorescence quenching studies. Copper interaction studies suggested that brazilein could bind with copper ions of the enzyme. Circular dichroism analysis confirmed that brazilein induced secondary structural changes in tyrosinase. Docking studies further authenticate that brazilein forms hydrophobic and hydrogen bonding with the active site residues of tyrosinase. Moreover, in vitro studies confirmed that the inhibitory mechanism of cellular tyrosinase and melanin synthesis by brazilein in B16F0 melanoma cells. These results suggested that brazilein act as a potential tyrosinase inhibitor and it would contribute as a of novel tyrosinase inhibitor in food, cosmetic and pharmaceutical industry.
authors.affiliation: School of Bio Sciences and Technology, VIT University, Vellore 632014, Tamil Nadu, India.
authors.forename: Hemachandran
authors.initials: H
authors.lastname: Hridya
authors.affiliation: School of Bio Sciences and Technology, VIT University, Vellore 632014, Tamil Nadu, India.
authors.forename: Anantharaman
authors.initials: A
authors.lastname: Amrita
authors.affiliation: School of Bio Sciences and Technology, VIT University, Vellore 632014, Tamil Nadu, India.
authors.forename: Mohan
authors.initials: M
authors.lastname: Sankari
authors.affiliation: School of Bio Sciences and Technology, VIT University, Vellore 632014, Tamil Nadu, India.
authors.forename: C
authors.initials: C
authors.lastname: George Priya Doss
authors.affiliation: School of Advanced Sciences, VIT University, Vellore 632014, Tamil Nadu, India.
authors.forename: Mohan
authors.initials: M
authors.lastname: Gopalakrishnan
authors.affiliation: School of Bio Sciences and Technology, VIT University, Vellore 632014, Tamil Nadu, India.
authors.forename: Chandrasekaran
authors.initials: C
authors.lastname: Gopalakrishnan
authors.affiliation: School of Bio Sciences and Technology, VIT University, Vellore 632014, Tamil Nadu, India. Electronic address: rsiva77in@rediffmail.com.
authors.forename: Ramamoorthy
authors.initials: R
authors.lastname: Siva
mesh_terms: D000818:Animals; D001578:Benzopyrans / Q000737:chemistry* / Q000494:pharmacology*; D002470:Cell Survival / Q000187:drug effects; D002851:Chromatography, High Pressure Liquid; D002942:Circular Dichroism; D003198:Computer Simulation; D003300:Copper / Q000737:chemistry; D004789:Enzyme Activation / Q000187:drug effects; D004791:Enzyme Inhibitors / Q000737:chemistry / Q000494:pharmacology; D007192:Indenes / Q000737:chemistry* / Q000494:pharmacology*; D007477:Ions / Q000737:chemistry; D007700:Kinetics; D008543:Melanins / Q000096:biosynthesis*; D008546:Melanoma, Experimental; D051379:Mice; D008968:Molecular Conformation; D062105:Molecular Docking Simulation; D014442:Monophenol Monooxygenase / Q000037:antagonists & inhibitors* / Q000737:chemistry*; D066244:Proton Magnetic Resonance Spectroscopy; D017550:Spectroscopy, Fourier Transform Infrared
chemical_list: D001578:Benzopyrans; D004791:Enzyme Inhibitors; D007192:Indenes; D007477:Ions; D008543:Melanins; C050295:brazilein; D003300:Copper; D014442:Monophenol Monooxygenase
keywords: Brazilein; Caesalpinia sappan; Tyrosinase