Methods for chemical inhibition of melanin synthesis

Melanin is a heteropolymeric pigment essential for protecting human skin from UV-visible radiation through broad-spectrum absorption. It is produced within melanocytes and stored in melanosomes. Melanogenesis begins with the activity of tyrosinase, a membrane-bound enzyme that converts L-tyrosine into DOPAquinone. Dysregulated tyrosinase activity contributes to several skin disorders, including hyperpigmentation, oxidative stress and an increased risk of malignant melanoma (Xinhua Ni, 2025). Over the years, extensive research has focused on understanding how tyrosinase functions and how its activity can be modulated. Numerous tyrosinase inhibitors have been identified and are now widely used in dermatology, cosmetology and clinical treatments for pigmentation disorders. These compounds act through different mechanisms; some directly inhibit tyrosinase, while others interfere with various steps of the melanogenesis pathway. This work aims to summarize the current knowledge on melanin synthesis and to examine key chemical inhibitors involved in its regulation, ranging from commonly used molecules such as glabridin and kojic acid to newer approaches including the cyclopeptide CHP-9 and salicylic acid. Several of these modulators have also shown potential in melanoma studies, highlighting their value not only in pigmentation control but also as possible therapeutic agents.