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Design, synthesis and bioevaluation of novel umbelliferone analogues as potential mushroom tyrosinase inhibitors.
J Enzyme Inhib Med Chem. 2015 Dec; 30(6):874-83.JE

Abstract

A series of umbelliferone analogues were synthesized and their inhibitory effects on the DPPH and mushroom tyrosinase were evaluated. The results showed that some of the synthesized compounds exhibited significant mushroom tyrosinase inhibitory activities. Especially, 2-oxo-2-[(2-oxo-2H-chromen-7-yl)oxy]ethyl-2,4-dihydroxybenzoate (4e) bearing 2,4-dihydroxy substituted phenyl ring exhibited the most potent tyrosinase inhibitory activity with IC50 value 8.96 µM and IC50 value of kojic acid is 16.69. The inhibition mechanism analyzed by Lineweaver-Burk plots revealed that the type of inhibition of compound 4e on tyrosinase was non-competitive. The docking study against tyrosinase enzyme was also performed to determine the binding affinity of the compounds. The compounds 4c and 4e showed the highest binding affinity with active binding site of tyrosinase. The initial structure activity relationships (SARs) analysis suggested that further development of such compounds might be of interest. The statistics of our results endorses that compounds 4c and 4e may serve as a structural template for the design and development of novel tyrosinase inhibitors.

Authors+Show Affiliations

a Department of Biology, College of Natural Sciences , Kongju National University , Kongju , South Korea . b Department of Chemistry , Allama Iqbal Open University , Islamabad , Pakistan , and.a Department of Biology, College of Natural Sciences , Kongju National University , Kongju , South Korea .a Department of Biology, College of Natural Sciences , Kongju National University , Kongju , South Korea .c Atta-ur-Rahman School of Applied Biosciences, National University of Sciences and Technology , Islamabad , Pakistan.c Atta-ur-Rahman School of Applied Biosciences, National University of Sciences and Technology , Islamabad , Pakistan.

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

25643758

Citation

Ashraf, Zaman, et al. "Design, Synthesis and Bioevaluation of Novel Umbelliferone Analogues as Potential Mushroom Tyrosinase Inhibitors." Journal of Enzyme Inhibition and Medicinal Chemistry, vol. 30, no. 6, 2015, pp. 874-83.
Ashraf Z, Rafiq M, Seo SY, et al. Design, synthesis and bioevaluation of novel umbelliferone analogues as potential mushroom tyrosinase inhibitors. J Enzyme Inhib Med Chem. 2015;30(6):874-83.
Ashraf, Z., Rafiq, M., Seo, S. Y., Babar, M. M., & Zaidi, N. U. (2015). Design, synthesis and bioevaluation of novel umbelliferone analogues as potential mushroom tyrosinase inhibitors. Journal of Enzyme Inhibition and Medicinal Chemistry, 30(6), 874-83. https://doi.org/10.3109/14756366.2014.979346
Ashraf Z, et al. Design, Synthesis and Bioevaluation of Novel Umbelliferone Analogues as Potential Mushroom Tyrosinase Inhibitors. J Enzyme Inhib Med Chem. 2015;30(6):874-83. PubMed PMID: 25643758.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Design, synthesis and bioevaluation of novel umbelliferone analogues as potential mushroom tyrosinase inhibitors. AU - Ashraf,Zaman, AU - Rafiq,Muhammad, AU - Seo,Sung-Yum, AU - Babar,Mustafeez Mujtaba, AU - Zaidi,Najam-Us-Sahar Sadaf, Y1 - 2015/02/03/ PY - 2015/2/4/entrez PY - 2015/2/4/pubmed PY - 2016/6/9/medline KW - Antioxidant activity KW - kinetic studies KW - molecular modeling KW - mushroom tyrosinase inhibitors KW - synthesis KW - umbelliferone analogues SP - 874 EP - 83 JF - Journal of enzyme inhibition and medicinal chemistry JO - J Enzyme Inhib Med Chem VL - 30 IS - 6 N2 - A series of umbelliferone analogues were synthesized and their inhibitory effects on the DPPH and mushroom tyrosinase were evaluated. The results showed that some of the synthesized compounds exhibited significant mushroom tyrosinase inhibitory activities. Especially, 2-oxo-2-[(2-oxo-2H-chromen-7-yl)oxy]ethyl-2,4-dihydroxybenzoate (4e) bearing 2,4-dihydroxy substituted phenyl ring exhibited the most potent tyrosinase inhibitory activity with IC50 value 8.96 µM and IC50 value of kojic acid is 16.69. The inhibition mechanism analyzed by Lineweaver-Burk plots revealed that the type of inhibition of compound 4e on tyrosinase was non-competitive. The docking study against tyrosinase enzyme was also performed to determine the binding affinity of the compounds. The compounds 4c and 4e showed the highest binding affinity with active binding site of tyrosinase. The initial structure activity relationships (SARs) analysis suggested that further development of such compounds might be of interest. The statistics of our results endorses that compounds 4c and 4e may serve as a structural template for the design and development of novel tyrosinase inhibitors. SN - 1475-6374 UR - https://www.unboundmedicine.com/medline/citation/25643758/Design_synthesis_and_bioevaluation_of_novel_umbelliferone_analogues_as_potential_mushroom_tyrosinase_inhibitors_ L2 - https://www.tandfonline.com/doi/full/10.3109/14756366.2014.979346 DB - PRIME DP - Unbound Medicine ER -