Exploration of Ferulic Acid and Its Derivatives as Potent Anti-Tyrosinase: A Systematic Review

Abstract

Tyrosinase is an enzyme that catalyzes melanin biosynthesis. Recently, it has become a popular target for developing cosmetics as a skin lightening or skin whitening agent, an anti-aging agent, an anti-wrinkle agent, and other therapeutics for skin disorders. Based on the previous reports, many compounds have been developed and designed to be tyrosinase inhibitors, including ferulic acid and cinnamic acid derivatives. However, until now, the use of these compounds in commercial cosmetic products has been limited. It may be due to chemical instability, lipophilicity, and poor efficacy. In this review, we assessed research studies to discuss the structure-activity of ferulic acid and its derivatives, which can contribute to their better efficacy as anti-tyrosinases. Either ferulic acid as a single compound or its hybridization with other cinnamic acid derivatives proved beneficial in designing tyrosinase inhibitors as active functional groups. The structure-activity of the phenyl ring's substituent improved inhibitory effects on monophenolase activity, especially the halogen substituent. In addition, the alkyl chain length and other functional groups linked, such as amide and acetyl groups, could alter the inhibitory properties, including hydrophobicity, to produce a more stable complex ligand-receptor.

Molecular Docking Studies of Ortho-Substituted Phenols to Tyrosinase Helps Discern If a Molecule Can Be an Enzyme Substrate

“…This is not true in the data described above, and therefore these compounds do not behave as pure competitive inhibitors; this inhibition is only apparent [21]. More recently, a review has been published on the action of FA and its derivatives as potent tyrosinase inhibitors, indicating that the inhibition capacity is due to the presence of double bond conjugation as a side chain in is molecule [22]. We, based on published data and those described in Figure 2, propose that FA is an alternative substrate of the enzyme [23].…”