Screening of inhibitors for mushroom tyrosinase using surface plasmon resonance

Tyrosinase inhibitors have been used as whitening or antihyperpigment agents because of their ability to suppress dermal-melanin production. In the present study, screening and kinetic evaluation of various small molecules were performed on mushroom tyrosinase (MT) using surface plasmon resonance. The binding constant KD (M) values obtained for tannic acid, phloroglucinol, saffron, catechol, and pyrogallol are 1.213 × 10(-4), 7.136 × 10(-5), 3.111 × 10(-5), 1.557 × 10(-5), and 7.981 × 10(-6) M, respectively. Pyrogallol has been found to display high affinity for MT, whereas catechol, saffron, and phloroglucinol have been found to bind with low affinity. MT shows considerable changes in the secondary structure in the presence of inhibitors. The study reveals the Biacore/SPR sensor's ability in the rapid identification and characterization of inhibitors for MT. The methodology described here can be used to rapidly screen and optimize various lead compounds for other enzymes and elucidate structure function inter-relationships between various enzymes.