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.
2011
46
2243
2251
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
File in questo prodotto:
File Dimensione Formato  
Paoli et al 2011.pdf

accesso aperto

Tipologia: Versione finale referata (Postprint, Accepted manuscript)
Licenza: Open Access
Dimensione 960.97 kB
Formato Adobe PDF
960.97 kB Adobe PDF

I documenti in FLORE sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificatore per citare o creare un link a questa risorsa: https://hdl.handle.net/2158/416057
Citazioni
  • ???jsp.display-item.citation.pmc??? ND
  • Scopus 104
  • ???jsp.display-item.citation.isi??? 100
social impact