Biomimetics | |
2-S-Lipoylcaffeic Acid, a Natural Product-Based Entry to Tyrosinase Inhibition via Catechol Manipulation | |
Valeria Pistorio1  Elio Pizzo1  Lucia Panzella2  Raffaella Micillo2  Alessandra Napolitano2  Marco d’Ischia2  | |
[1] Department of Biology, University of Naples “Federico II”, Via Cintia 4, I-80126 Naples, Italy;Department of Chemical Sciences, University of Naples “Federico II”, Via Cintia 4, I-80126 Naples, Italy; | |
关键词: depigmenting agents; ">l-DOPA; dopachrome; tyrosinase; melanin; caffeic acid; dihydrolipoic acid; lipoic acid; keratinocytes; | |
DOI : 10.3390/biomimetics2030015 | |
来源: DOAJ |
【 摘 要 】
Conjugation of naturally occurring catecholic compounds with thiols is a versatile and facile entry to a broad range of bioinspired multifunctional compounds for diverse applications in biomedicine and materials science. We report herein the inhibition properties of the caffeic acid- dihydrolipoic acid S-conjugate, 2-S-lipoylcaffeic acid (LC), on mushroom tyrosinase. Half maximum inhibitory concentration (IC50) values of 3.22 ± 0.02 and 2.0 ± 0.1 µM were determined for the catecholase and cresolase activity of the enzyme, respectively, indicating a greater efficiency of LC compared to the parent caffeic acid and the standard inhibitor kojic acid. Analysis of the Lineweaver–Burk plot suggested a mixed-type inhibition mechanism. LC proved to be non-toxic on human keratinocytes (HaCaT) at concentrations up to 30 µM. These results would point to LC as a novel prototype of melanogenesis regulators for the treatment of pigmentary disorders.
【 授权许可】
Unknown