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Condensed tannins from Ficus virens as tyrosinase inhibitors: structure, inhibitory activity and molecular mechanism.
PLoS One. 2014; 9(3):e91809.Plos

Abstract

Condensed tannins from Ficus virens leaves, fruit, and stem bark were isolated and their structures characterized by 13C nuclear magnetic resonance spectrometry, high performance liquid chromatography electrospray ionization mass spectrometry, and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. The results showed that the leaves, fruit, and stem bark condensed tannins were complex mixtures of homo- and heteropolymers of B-type procyanidins and prodelphinidins with degrees of polymerization up to hexamer, dodecamer, and pentadecamer, respectively. Antityrosinase activities of the condensed tannins were studied. The results indicated that the condensed tannins were potent tyrosinase inhibitors. The concentrations for the leaves, fruit, and stem bark condensed tannins leading to 50% enzyme activity were determined to be 131.67, 99.89, and 106.22 μg/ml on monophenolase activity, and 128.42, 43.07, and 74.27 μg/ml on diphenolase activity. The inhibition mechanism, type, and constants of the condensed tannins on the diphenolase activity were further investigated. The results indicated that the condensed tannins were reversible and mixed type inhibitors. Fluorescence quenching, copper interacting, and molecular docking techniques were utilized to unravel the molecular mechanisms of the inhibition. The results showed that the hydroxyl group on the B ring of the condensed tannins could chelate the dicopper irons of the enzyme. Moreover, the condensed tannins could reduce the enzyme product o-quinones into colourless compounds. These results would contribute to the development and design of antityrosinase agents.

Authors+Show Affiliations

Key Lab of the Ministry of Education for Coastal and Wetland Ecosystems, School of Life Sciences, Xiamen University, Xiamen, China.Key Lab of the Ministry of Education for Coastal and Wetland Ecosystems, School of Life Sciences, Xiamen University, Xiamen, China.Key Lab of the Ministry of Education for Coastal and Wetland Ecosystems, School of Life Sciences, Xiamen University, Xiamen, China.Key Lab of the Ministry of Education for Coastal and Wetland Ecosystems, School of Life Sciences, Xiamen University, Xiamen, China.Fujian Provincial Key Laboratory of Neurodegenerative Disease and Aging Research, College of Medicine, Xiamen University, Xiamen, China.Key Lab of the Ministry of Education for Coastal and Wetland Ecosystems, School of Life Sciences, Xiamen University, Xiamen, China.

Pub Type(s)

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

Language

eng

PubMed ID

24637701

Citation

Chen, Xiao-Xin, et al. "Condensed Tannins From Ficus Virens as Tyrosinase Inhibitors: Structure, Inhibitory Activity and Molecular Mechanism." PloS One, vol. 9, no. 3, 2014, pp. e91809.
Chen XX, Shi Y, Chai WM, et al. Condensed tannins from Ficus virens as tyrosinase inhibitors: structure, inhibitory activity and molecular mechanism. PLoS One. 2014;9(3):e91809.
Chen, X. X., Shi, Y., Chai, W. M., Feng, H. L., Zhuang, J. X., & Chen, Q. X. (2014). Condensed tannins from Ficus virens as tyrosinase inhibitors: structure, inhibitory activity and molecular mechanism. PloS One, 9(3), e91809. https://doi.org/10.1371/journal.pone.0091809
Chen XX, et al. Condensed Tannins From Ficus Virens as Tyrosinase Inhibitors: Structure, Inhibitory Activity and Molecular Mechanism. PLoS One. 2014;9(3):e91809. PubMed PMID: 24637701.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Condensed tannins from Ficus virens as tyrosinase inhibitors: structure, inhibitory activity and molecular mechanism. AU - Chen,Xiao-Xin, AU - Shi,Yan, AU - Chai,Wei-Ming, AU - Feng,Hui-Ling, AU - Zhuang,Jiang-Xing, AU - Chen,Qing-Xi, Y1 - 2014/03/17/ PY - 2013/12/02/received PY - 2014/02/14/accepted PY - 2014/3/19/entrez PY - 2014/3/19/pubmed PY - 2015/1/15/medline SP - e91809 EP - e91809 JF - PloS one JO - PLoS One VL - 9 IS - 3 N2 - Condensed tannins from Ficus virens leaves, fruit, and stem bark were isolated and their structures characterized by 13C nuclear magnetic resonance spectrometry, high performance liquid chromatography electrospray ionization mass spectrometry, and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. The results showed that the leaves, fruit, and stem bark condensed tannins were complex mixtures of homo- and heteropolymers of B-type procyanidins and prodelphinidins with degrees of polymerization up to hexamer, dodecamer, and pentadecamer, respectively. Antityrosinase activities of the condensed tannins were studied. The results indicated that the condensed tannins were potent tyrosinase inhibitors. The concentrations for the leaves, fruit, and stem bark condensed tannins leading to 50% enzyme activity were determined to be 131.67, 99.89, and 106.22 μg/ml on monophenolase activity, and 128.42, 43.07, and 74.27 μg/ml on diphenolase activity. The inhibition mechanism, type, and constants of the condensed tannins on the diphenolase activity were further investigated. The results indicated that the condensed tannins were reversible and mixed type inhibitors. Fluorescence quenching, copper interacting, and molecular docking techniques were utilized to unravel the molecular mechanisms of the inhibition. The results showed that the hydroxyl group on the B ring of the condensed tannins could chelate the dicopper irons of the enzyme. Moreover, the condensed tannins could reduce the enzyme product o-quinones into colourless compounds. These results would contribute to the development and design of antityrosinase agents. SN - 1932-6203 UR - https://www.unboundmedicine.com/medline/citation/24637701/Condensed_tannins_from_Ficus_virens_as_tyrosinase_inhibitors:_structure_inhibitory_activity_and_molecular_mechanism_ L2 - https://dx.plos.org/10.1371/journal.pone.0091809 DB - PRIME DP - Unbound Medicine ER -