In vitro and in silico investigation of tyrosinase and alpha amylase inhibition potentials of some new organic compounds

In this study, the inhibition potential, IC50 values, inhibition type and Ki values of compounds containing some piperazine, 1,2,4-triazole and/or fluoroquinolone structures on clinically important tyrosinase and α-amylase enzymes were investigated. Theoretically, molecular modeling programs were used to determine the interaction of these compounds with enzymes and their binding energies. After determining the optimum reaction conditions for commercially available enzymes, kinetic studies were carried out and the molecules with the lowest IC50 value were determined as 7th molecule for tyrosinase and 5th molecule for α-amylase. The inhibition mechanism for the 7th molecule is noncompetitive, while the Ki value is 477.86 µM, the inhibition mechanism for 5th molecule is uncompetitive and the Ki value was determined to be 355.84 µM. According to molecular modeling results, molecules with the lowest active site binding energy were observed as 5th molecule for tyrosinase and 6th molecule for α-amylase. In addition, in vitro studies, it has been observed that molecules showing a high inhibition profile are one of the three most effective molecules in silico studies in both enzyme states. ADME properties of all studied molecules were also examined, and it was determined that each molecule has a high potential as a drug candidate molecule. As a result of the studies, it is predicted that the 7th molecule and 5th molecules, may be potential inhibitors for tyrosinase and α-amylase, respectively.