Abstract: The aim of the current study was to investigate the oral antidiabetic activity of four structurally-related tri- terpenic acids: ursolic (RE-01), oleanolic (RE-02), moronic (RE-03) and morolic (RE-04) acids. STZ-nicotin- amide diabetic rats were treated with these triterpenes (50 mg/kg) and the antidiabetic effects in acute experiment were determined. All compounds showed significant antidiabetic activity in comparison with control group(p<0.05). The invitro inhibitoryactivityof compounds againstproteintyrosinephosphatase1B (PTPe1B) was also evaluated. At 50 M, the enzymatic activity was almost completely inhibited. All compoundswere dockedwith a crystal structure of PTPe1B.Docking results suggested the potential binding of the triterpenic acids ina bindingpocketnext tothe catalytic site.Anextensivehydrogenbondnetworkwith the carboxyl group and Van derWaals interactions stabilize the protein-ligand complexes.
Antidiabetic activity of some pentacyclic acid triterpenoids, role of PTPe1B: In vitro, in silico, and in vivo approaches / J.J. Ramírez-Espinosa; M.Y. Ríos; S. López-Martínez; F. López-Vallejo; J.L. Medina-Franco; P. Paoli; G. Camici; G. Navarrete-Vázquez; R. Ortiz-Andrade; S. Estrada-Soto. - In: EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY. - ISSN 0223-5234. - STAMPA. - 46:(2011), pp. 2243-2251. [10.1016/j.ejmech.2011.03.005]
Antidiabetic activity of some pentacyclic acid triterpenoids, role of PTPe1B: In vitro, in silico, and in vivo approaches
PAOLI, PAOLO;CAMICI, GUIDO;
2011
Abstract
Abstract: The aim of the current study was to investigate the oral antidiabetic activity of four structurally-related tri- terpenic acids: ursolic (RE-01), oleanolic (RE-02), moronic (RE-03) and morolic (RE-04) acids. STZ-nicotin- amide diabetic rats were treated with these triterpenes (50 mg/kg) and the antidiabetic effects in acute experiment were determined. All compounds showed significant antidiabetic activity in comparison with control group(p<0.05). The invitro inhibitoryactivityof compounds againstproteintyrosinephosphatase1B (PTPe1B) was also evaluated. At 50 M, the enzymatic activity was almost completely inhibited. All compoundswere dockedwith a crystal structure of PTPe1B.Docking results suggested the potential binding of the triterpenic acids ina bindingpocketnext tothe catalytic site.Anextensivehydrogenbondnetworkwith the carboxyl group and Van derWaals interactions stabilize the protein-ligand complexes.File | Dimensione | Formato | |
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