Institute of Biomolecular Chemistry of CNR, Padova Unit, Via F. Marzolo, 1, 35131 Padova, Italy.
Institute of Biomolecular Chemistry of CNR, Sassari Unit, Traversa La Crucca, 3, 07100 Sassari, Italy.
Int J Mol Sci. 2022 Jun 2;23(11):6240. doi: 10.3390/ijms23116240.
The tyrosinase enzyme, which catalyzes the hydroxylation of monophenols and the oxidation of -diphenols, is typically involved in the synthesis of the dark product melanin starting from the amino acid tyrosine. Contributing to the browning of plant and fruit tissues and to the hyperpigmentation of the skin, leading to melasma or age spots, the research of possible tyrosinase inhibitors has attracted much interest in agri-food, cosmetic, and medicinal industries. In this study, we analyzed the capability of antamanide, a mushroom bioactive cyclic decapeptide, and some of its glycine derivatives, compared to that of pseudostellarin A, a known tyrosinase inhibitor, to hinder tyrosinase activity by using a spectrophotometric method. Additionally, computational docking studies were performed in order to elucidate the interactions occurring with the tyrosinase catalytic site. Our results show that antamanide did not exert any inhibitory activity. On the contrary, the three glycine derivatives , , and , which differ from each other by the position of a glycine that substitutes phenylalanine in the parent molecule, improving water solubility and flexibility, showed tyrosinase inhibition by spectrophotometric assays. Analytical data were confirmed by computational studies.
酪氨酸酶能够催化单酚的羟化和 -二酚的氧化，通常参与从氨基酸酪氨酸开始合成深色产物黑色素。酪氨酸酶的研究在农业食品、化妆品和医药行业引起了广泛关注，因为它会导致植物和果实组织的褐变和皮肤的色素沉着过度，导致黄褐斑或老年斑。在这项研究中，我们使用分光光度法分析了蘑菇生物活性环十肽 antamanide 及其一些甘氨酸衍生物与已知的酪氨酸酶抑制剂 pseudostellarin A 抑制酪氨酸酶活性的能力。此外，还进行了计算对接研究，以阐明与酪氨酸酶催化位点发生的相互作用。我们的结果表明，antamanide 没有表现出任何抑制活性。相反，三个甘氨酸衍生物 、 、和 ，它们通过取代母体分子中苯丙氨酸的甘氨酸的位置而彼此不同，提高了水溶性和灵活性，通过分光光度法测定显示出对酪氨酸酶的抑制作用。计算研究证实了分析数据。
