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  3. Nitrophenylpiperazine derivatives as novel tyrosinase inhibitors: design, synthesis, and in silico evaluations

Nitrophenylpiperazine derivatives as novel tyrosinase inhibitors: design, synthesis, and in silico evaluations

  • BMC Chem. 2024 Apr 5;18(1):67. doi: 10.1186/s13065-024-01167-6.
Mehdi Asadi 1,  Fahime Fayazi 2,  Aida Iraji 3 4,  Reyhaneh Sabourian 5,  Homa Azizian 1,  Mannan Hajimahmoodi 5,  Bagher Larijani 6,  Mohammad Mahdavi 7,  Massoud Amanlou 8 9
Affiliations

Affiliations

  • 1 Department of Medicinal Chemistry, School of Pharmacy, Iran University of Medical Sciences, Tehran, Iran.
  • 2 Department of Medicinal Chemistry, Faculty of Pharmacy, Tehran University of Medical Sciences, Tehran, Iran.
  • 3 Stem Cells Technology Research Center, Shiraz University of Medical Sciences, Shiraz, Iran.
  • 4 Central Research Laboratory, Shiraz University of Medical Sciences, Shiraz, Iran.
  • 5 Drug and Food Control Department, Faculty of Pharmacy, Tehran University of Medical Sciences, Tehran, Iran.
  • 6 Endocrinology and Metabolism Research Center, Endocrinology and Metabolism Clinical Sciences Institute, Tehran University of Medical Sciences, Tehran, Islamic Republic of Iran.
  • 7 Endocrinology and Metabolism Research Center, Endocrinology and Metabolism Clinical Sciences Institute, Tehran University of Medical Sciences, Tehran, Islamic Republic of Iran. mahdavi_chem@yahoo.com.
  • 8 Department of Medicinal Chemistry, Faculty of Pharmacy, Tehran University of Medical Sciences, Tehran, Iran. amanlou@tums.ac.ir.
  • 9 Experimental Medicine Research Center, Tehran University of Medical Sciences, Tehran, Iran. amanlou@tums.ac.ir.
PMID: 38581040 DOI: 10.1186/s13065-024-01167-6
Abstract

A novel series of 4-nitrophenylpiperazine derivatives (4a-m) was designed and synthesized as potential Tyrosinase inhibitors. Comprehensive characterization using 1H-NMR, 13C-NMR, CNH, and IR techniques was performed for all target compounds. Subsequently, the derivatives were evaluated for their inhibitory activity against Tyrosinase. Among them, compound 4l, featuring an indole moiety at the N-1 position of the piperazine ring, exhibited a significant Tyrosinase inhibitory effect with an IC50 value of 72.55 μM. Enzyme kinetics analysis revealed that 4l displayed mixed inhibition of the Tyrosinase enzymatic reaction. Molecular docking was carried out in the enzyme's active site to further investigate the enzyme-inhibitor interactions. Based on the findings, compound 4l shows promise as a lead structure for the design of potent Tyrosinase inhibitors. This study paves the way for the development of more effective Tyrosinase inhibitors for potential applications in various fields.

Keywords

Docking studies; Kinetic evaluation; Nitrophenylpiperazine; Synthesis; Tyrosinase inhibitors.

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