ArticleInternational journal of molecular sciences2025
Synthesis, Antimicrobial Activity, and Tyrosinase Inhibition by Multifunctional 3,4-Dihydroxy-Phenyl Peptidomimetics.
Article in International journal of molecular sciences, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
1 citing paper in PubMed.
- Tyrosinase Inhibitors With Enhanced Potency in Mammalian and Vertebrate Models, N-(2-Mercaptoethyl)benzamide Derivatives: Design, Synthesis, and Evaluation.Chemical biology & drug design · 2026Article
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5 authors.
Funding
Abstract
The purpose of the present study was to evaluate the synergistic effect of two important pharmacophores, 3,4-dihydroxyphenyl and peptidomimetic moieties, as mushroom tyrosinase inhibitors and antimicrobial agents targeting specific strains of pathogenic bacteria. The 3,4-dihydroxybenzaldehyde (protocatechuic aldehyde) was found to be an effective inhibitor of tyrosinase activity, and due to the fact that it is a safe natural substance with such a scaffolded structure, it is likely that dihydroxyl-substituted phenolic derivatives can exhibit potent tyrosinase inhibitory activity. Series of peptidomimetics with an incorporated 3,4-dihydroxyphenyl scaffold was synthesized and characterized. The inhibitory effects of peptidomimetics on a mushroom tyrosinase were studied. The results showed that among the compounds, five of them showed higher inhibitory activity than the parent 3,4-dihydroxybenzyl aldehyde. In silico docking studies with mushroom tyrosinase (PDB ID 2Y9X) predicted possible binding modes in the enzymatic pocket for these compounds. Furthermore, the antimicrobial activities of peptidomimetics against selected Gram-positive and Gram-negative bacterial strains (
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