Abstract
Studies on tyrosinase have recently gained the attention of researchers due to the enzyme's biological functions and potential applications in food and cosmetic applications. In this present study, screening and kinetic evaluation of small molecules (>300Da) on human tyrosinase was carried out using surface plasmon resonance and molecular docking studies. Four molecules showed significant binding were further characterized. The binding constant KD (M) values obtained for crocin, curcumin, tannic acid, pyrogallol and hydroquinone are 5.60×10-5, 1.52×10-3, 6.45×10-5, 1.34×10-5 and 2.433×10-7M respectively. In silico docking studies using autodock indicated significant binding and revealed the binding pocket residues for all molecules. The study shows the Biacore/SPR sensor's ability for screening and detection of inhibitors for human tyrosinase. This study can be used to rapidly screen and optimize various lead compounds as binders/inhibitors/modulators of human tyrosinase enzyme activity.