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Synthesis, molecular docking studies of coumarinyl-pyrazolinyl substituted thiazoles as non-competitive inhibitors of mushroom tyrosinase.
Bioorg Chem. 2017 10; 74:187-196.BC

Abstract

A series of coumarinyl-pyrazolinyl substituted thiazoles derivatives were synthesized and their inhibitory effects on the DPPH and mushroom tyrosinase were evaluated. The results showed that all of the synthesized compounds exhibited significant mushroom tyrosinase inhibitory activities. In particular, 3-(5-(4-(benzyloxy)-3-methoxyphenyl)-1-(4-(4-bromophenyl)thiazol-2-yl)-4,5-dihydro-1H-pyrazol-3-yl)-2H-chromen-2-one (7j) exhibited the most potent tyrosinase inhibitory activity with IC50 value 0.00458±0.00022μM compared with the IC50 value of kojic acid is 16.84±0.052μM. The inhibition mechanism analyzed by Lineweaver-Burk plots revealed that the type of inhibition of compound 7j on tyrosinase was noncompetitive. The docking study against tyrosinase enzyme was also performed to determine the binding affinity of the compounds. The compound 7a showed the highest binding affinity (-10.20kcal/mol) 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 compound 7j may serve asa structural template for the design and development of novel tyrosinase inhibitors.

Authors+Show Affiliations

Department of Chemistry, Quaid-I-Azam University, Islamabad 45320, Pakistan. Electronic address: aamersaeed@yahoo.com.Department of Chemistry, Quaid-I-Azam University, Islamabad 45320, Pakistan.Department of Chemistry, Quaid-I-Azam University, Islamabad 45320, Pakistan.Department of Biological Sciences, College of Natural Sciences, Kongju National University, 56 Gongjudehak-Ro, Gongju, Chungnam 314-701, Republic of Korea; Department of Physiology, University of Sindh, Jamshoro 76080, Pakistan.Department of Chemistry, Quaid-I-Azam University, Islamabad 45320, Pakistan. Electronic address: fayazali@chem.qau.edu.pk.Department of Biological Sciences, College of Natural Sciences, Kongju National University, 56 Gongjudehak-Ro, Gongju, Chungnam 314-701, Republic of Korea.Department of Biological Sciences, College of Natural Sciences, Kongju National University, 56 Gongjudehak-Ro, Gongju, Chungnam 314-701, Republic of Korea.Department of Biological Sciences, College of Natural Sciences, Kongju National University, 56 Gongjudehak-Ro, Gongju, Chungnam 314-701, Republic of Korea.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

28837887

Citation

Saeed, Aamer, et al. "Synthesis, Molecular Docking Studies of Coumarinyl-pyrazolinyl Substituted Thiazoles as Non-competitive Inhibitors of Mushroom Tyrosinase." Bioorganic Chemistry, vol. 74, 2017, pp. 187-196.
Saeed A, Mahesar PA, Channar PA, et al. Synthesis, molecular docking studies of coumarinyl-pyrazolinyl substituted thiazoles as non-competitive inhibitors of mushroom tyrosinase. Bioorg Chem. 2017;74:187-196.
Saeed, A., Mahesar, P. A., Channar, P. A., Abbas, Q., Larik, F. A., Hassan, M., Raza, H., & Seo, S. Y. (2017). Synthesis, molecular docking studies of coumarinyl-pyrazolinyl substituted thiazoles as non-competitive inhibitors of mushroom tyrosinase. Bioorganic Chemistry, 74, 187-196. https://doi.org/10.1016/j.bioorg.2017.08.002
Saeed A, et al. Synthesis, Molecular Docking Studies of Coumarinyl-pyrazolinyl Substituted Thiazoles as Non-competitive Inhibitors of Mushroom Tyrosinase. Bioorg Chem. 2017;74:187-196. PubMed PMID: 28837887.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Synthesis, molecular docking studies of coumarinyl-pyrazolinyl substituted thiazoles as non-competitive inhibitors of mushroom tyrosinase. AU - Saeed,Aamer, AU - Mahesar,Parvez Ali, AU - Channar,Pervaiz Ali, AU - Abbas,Qamar, AU - Larik,Fayaz Ali, AU - Hassan,Mubashir, AU - Raza,Hussain, AU - Seo,Sung-Yum, Y1 - 2017/08/12/ PY - 2017/03/10/received PY - 2017/07/30/revised PY - 2017/08/11/accepted PY - 2017/8/25/pubmed PY - 2017/10/11/medline PY - 2017/8/25/entrez KW - Antioxidant activity KW - Hybrid pharmacophore approach KW - Kinetic studies KW - Molecular docking KW - Mushroom tyrosinase inhibitors KW - Synthesis SP - 187 EP - 196 JF - Bioorganic chemistry JO - Bioorg. Chem. VL - 74 N2 - A series of coumarinyl-pyrazolinyl substituted thiazoles derivatives were synthesized and their inhibitory effects on the DPPH and mushroom tyrosinase were evaluated. The results showed that all of the synthesized compounds exhibited significant mushroom tyrosinase inhibitory activities. In particular, 3-(5-(4-(benzyloxy)-3-methoxyphenyl)-1-(4-(4-bromophenyl)thiazol-2-yl)-4,5-dihydro-1H-pyrazol-3-yl)-2H-chromen-2-one (7j) exhibited the most potent tyrosinase inhibitory activity with IC50 value 0.00458±0.00022μM compared with the IC50 value of kojic acid is 16.84±0.052μM. The inhibition mechanism analyzed by Lineweaver-Burk plots revealed that the type of inhibition of compound 7j on tyrosinase was noncompetitive. The docking study against tyrosinase enzyme was also performed to determine the binding affinity of the compounds. The compound 7a showed the highest binding affinity (-10.20kcal/mol) 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 compound 7j may serve asa structural template for the design and development of novel tyrosinase inhibitors. SN - 1090-2120 UR - https://www.unboundmedicine.com/medline/citation/28837887/Synthesis_molecular_docking_studies_of_coumarinyl_pyrazolinyl_substituted_thiazoles_as_non_competitive_inhibitors_of_mushroom_tyrosinase_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0045-2068(17)30161-X DB - PRIME DP - Unbound Medicine ER -