Design, synthesis and biological evaluation of oxindole-based chalcones as small-molecule inhibitors of melanogenic tyrosinase

Sharad Kumar Suthar, Sumit Bansal, Niteen Narkhede, Manju Guleria, Angel Treasa Alex, Alex Joseph

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

The enzyme tyrosinase regulates melanogenesis and skin hyperpigmentation by converting L-3,4-dihy-droxyphenylalanine (L-DOPA) into dopaquinone, a key step in the melanin biosynthesis. The present work deals with design and synthesis of various oxindole-based chalcones as monophenolase and diphenolase activity inhibitors of tyrosinase. Among the screened compounds, 4-hydroxy-3-methoxybenzylidene moiety bearing chalcone (7) prepared by one pot reaction of oxindole and vanillin displayed the highest activity against tyrosinase with IC50s of 63.37 and 59.71µM in monophenolase and diphenolase activity assays, respectively. In molecular docking studies, chalcone 7 also showed the highest binding affinity towards the enzyme tyrosinase while exhibiting the lowest estimated free energy of binding, among all the ligands docked.

Original languageEnglish
Pages (from-to)833-839
Number of pages7
JournalChemical and Pharmaceutical Bulletin
Volume65
Issue number9
DOIs
Publication statusPublished - 2017

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All Science Journal Classification (ASJC) codes

  • Chemistry(all)
  • Drug Discovery

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