A small collection of C2-symmetry hydroxylated biphenyls was prepared by straightforward methods and the capability to act as inhibitors of tyrosinase has been evaluated by both spectrophotometric and electrochemical assays. Our attention was focused on the diphenolase activity of this enzyme characterized by the absence of the characteristic lag time of enzymatic reaction of its monophenolase activity. To this purpose, we evaluated the capability of tyrosinase to oxidize a natural o-diphenol substrate to o-quinone analyzing the changes in the UV-Vis spectrum of a solution of caffeic acid and the reduction of the cathodic current in a tyrosinase biosensor, respectively. Results of both the methods were comparable. Most of the compounds possessed higher inhibitory activity compared to compound 1, a known hydroxylated biphenyl inhibitor of tyrosinase.
Hydroxylated biphenyls as tyrosinase inhibitor: A spectrophotometric and electrochemical study
Ruzza Paolo;Fabbri Davide;Dettori Maria Antonietta;Delogu Giovanna
2017
Abstract
A small collection of C2-symmetry hydroxylated biphenyls was prepared by straightforward methods and the capability to act as inhibitors of tyrosinase has been evaluated by both spectrophotometric and electrochemical assays. Our attention was focused on the diphenolase activity of this enzyme characterized by the absence of the characteristic lag time of enzymatic reaction of its monophenolase activity. To this purpose, we evaluated the capability of tyrosinase to oxidize a natural o-diphenol substrate to o-quinone analyzing the changes in the UV-Vis spectrum of a solution of caffeic acid and the reduction of the cathodic current in a tyrosinase biosensor, respectively. Results of both the methods were comparable. Most of the compounds possessed higher inhibitory activity compared to compound 1, a known hydroxylated biphenyl inhibitor of tyrosinase.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
