Comparative analysis of the inhibitory effects of aloin on tyrosinase supported by Fe3O4@rGO: investigation of interaction mechanisms, inhibitory activity, and conformational changes†
*a
and
Yongnian
Ni
a
Abstract
Tyrosinase is a key enzyme that regulates the rate of melanin synthesis, thereby modulating both food browning and skin pigmentation. It has been found that aloin is an effective inhibitor of tyrosinase activity and Fe3O4@rGO has remarkable drug-loading capability. In this study, enzyme inhibition kinetics and multispectral techniques were employed to investigate the enzyme inhibitory effect of Fe3O4@rGO-aloin nanocomposites and evaluate their anti-browning effect and safety. The binding ability of tyrosinase and aloin was further enhanced by the addition of Fe3O4@rGO. The IC50 value of Fe3O4@rGO-aloin against tyrosinase was determined to be 2.26 ± 0.15 × 10−5 mol L−1 with a typical anticompetitive inhibition. The findings suggest that Fe3O4@rGO-aloin exhibits a more potent inhibitory effect on tyrosinase compared to aloin. Furthermore, three-dimensional fluorescence, Fourier transform infrared and circular dichroism experiments demonstrated that aloin-loaded Fe3O4@rGO nanoparticles induce alterations in the secondary structure and conformation of tyrosinase. This indicates the potential of Fe3O4@rGO nanocomposites as candidates for the development of novel tyrosinase inhibitors for the treatment of hyperpigmentation disorders.
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