Screening and identification of tyrosinase inhibitors in edible plant materials by on-line UPLC-enzyme reactor coupled with UHPLC-FTMS

Fang, Xiaoping; Dai, Lei; Ding, Tian-Ming; Zhu, Yan; Zan, Jun-Feng; Chen, Linlin; Ding, Xuehua; Liu, Junfeng

doi:10.1016/j.foodchem.2022.134331

Cited by 9 publications

(1 citation statement)

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“…Both elevated and low tyrosine levels in biological fluids are associated with many metabolic disorders. The browning of fruits and fungi after the harvest of crops such as mushrooms and that of beverages are also due to an abnormal level of tyrosine in plants [ 6 ]. Women are vulnerable to dermatological disorders such as freckles, senile lentigo, pigmented acne scars, and melasma, and these hyper-pigmentation conditions are directly associated with hyper-accumulation of melanin [ 7 ].…”

Section: Introductionmentioning

confidence: 99%

Synergistic Biomedical Potential and Molecular Docking Analyses of Coumarin–Triazole Hybrids as Tyrosinase Inhibitors: Design, Synthesis, In Vitro Profiling, and In Silico Studies

Kausar,

Zahoor,

Tabassum

et al. 2024

Pharmaceuticals

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The tyrosinase enzyme has a vital role in the browning of vegetables and fruits and the biosynthesis of melanin. In this work, we synthesized a diverse library of coumarin–triazole hybrids, and these compounds were characterized by using suitable analytical techniques. Our research work extends beyond the synthetic effort to explore the therapeutic potential of these compounds. We put the synthesized compounds through meticulous in vitro screening against the tyrosinase enzyme, and these coumarin derivatives evinced good IC50 values in the range of 0.339 ± 0.25 µM to 14.06 ± 0.92 µM. In the library of synthesized compounds, six compounds were found to be more potent than standard ascorbic acid (IC50 = 11.5 ± 1.00), and among them, 17e and 17f, being the most active, exhibited remarkable anti-tyrosinase potential, with IC50 values of 0.339 ± 0.25 μM and 3.148 ± 0.23 μM, respectively. Furthermore, an in silico modeling study was carried out to determine the key interactions of these compounds with the tyrosinase protein (PDB ID: 2Y9X) and thus to authenticate our experimental findings. The quantitative SAR studies exhibited a good correlation between the synthesized derivatives of coumarin and their anti-tyrosinase activity. The docking studies verified the experimental results, and ligand 17e showed good interaction with the core residues of tyrosinase. This study not only expands the field of coumarin–triazole hybrid synthesis but also provides valuable insights for the development of novel tyrosinase inhibitors.

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Section: Introductionmentioning

confidence: 99%