Xanthium strumarium as an Inhibitor of α-Glucosidase, Protein Tyrosine Phosphatase 1β, Protein Glycation and ABTS for Diabetic and Its ComplicationReportar como inadecuado


Xanthium strumarium as an Inhibitor of α-Glucosidase, Protein Tyrosine Phosphatase 1β, Protein Glycation and ABTS  for Diabetic and Its Complication


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Department of Food Science and Nutrition, Hallym University, 1 Hallymdeahak-gil, Chuncheon 24252, Korea





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Academic Editors: Dong-Kug Choi and Palanivel Ganesan

Abstract Phytochemical investigation of the natural products from Xanthium strumarium led to the isolation of fourteen compounds including seven caffeoylquinic acid CQA derivatives. The individual compounds were screened for inhibition of α-glucosidase, protein tyrosine phosphatase 1β PTP1β, advanced glycation end products AGEs, and ABTS+ radical scavenging activity using in vitro assays. Among the isolated compounds, methyl-3,5-di-caffeoyquinic acid exhibited significant inhibitory activity against α-glucosidase 18.42 μM, PTP1β 1.88 μM, AGEs 82.79 μM, and ABTS+ 6.03 μM. This effect was marked compared to that of the positive controls acarbose 584.79 μM, sumarin 5.51 μM, aminoguanidine 1410.00 μM, and trolox 29.72 μM respectively. In addition, 3,5-di-O-CQA 88.14 μM and protocatechuic acid 32.93 μM had a considerable inhibitory effect against α-glucosidase and ABTS+. Based on these findings, methyl-3,5-di-caffeoyquinic acid was assumed to be potentially responsible for the anti-diabetic actions of X. strumarium. View Full-Text

Keywords: Xanthium strumarium; methyl-3,5-di-caffeoyquinic acid; protein tyrosine phosphatase 1β; α-glucosidase; advanced glycation end products Xanthium strumarium; methyl-3,5-di-caffeoyquinic acid; protein tyrosine phosphatase 1β; α-glucosidase; advanced glycation end products





Autor: Seung Hwan Hwang, Zhiqiang Wang, Ha Na Yoon and Soon Sung Lim *

Fuente: http://mdpi.com/



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