Author | Gonzaga, Daniel | |
Author | Senger, Mario Roberto | |
Author | Da Silva, Fernando de Carvalho | |
Author | Ferreira, Vitor Francisco | |
Author | Silva, Floriano Paes | |
Access date | 2015-04-06T17:18:21Z | |
Available date | 2015-04-06T17:18:21Z | |
Document date | 2014 | pt_BR |
Citation | GONZAGA, Daniel; et al. 1-phenyl-1h- and 2-phenyl-2h-1,2,3-triazol derivatives: design, synthesis and inhibitory effect on alpha-glycosidases. European Journal of Medicinal Chemistry, v.74, p. 461-476,2014. | pt_BR |
ISSN | 02235234 | pt_BR |
URI | https://www.arca.fiocruz.br/handle/icict/9894 | |
Language | eng | pt_BR |
Publisher | Elsevier | pt_BR |
Rights | restricted access | pt_BR |
Title | 1-Phenyl-1H- and 2-phenyl-2H-1,2,3-triazol derivatives: Design, synthesis and inhibitory effect on alpha-glycosidases | pt_BR |
Type | Article | pt_BR |
DOI | DOI:10.1016/j.ejmech.2013.12.039 | pt_BR |
Abstract | Due to aging and increasingly overweight in human population, the incidence of non-insulin dependent
diabetes mellitus (NIDDM or Type 2 DM) is increasing considerably. Therefore, searching for new aglycosidase
inhibitors (GIs) capable of slowing down carbohydrate assimilation by humans is an
important strategy towards control of NIDDM. In this report, we disclose the search for new easily
accessible synthetic triazoles as anti-diabetic compounds. Two series of non-glycosid triazoles were
synthesized (series A and B) and screened against baker’s yeast a-glucosidase (MAL12) and porcine
pancreatic a-amylase activity (PPA). Of the 60 compounds tested at 500 mM, were considered hits ( 60%
inhibition) six triazoles against MAL12 and three against PPA, with the inhibition reaching up to 99.4% on
MAL12 and 88.6% on PPA. The IC50 values were calculated for both enzymes and ranged from 54 to
482 mM for MAL12 and 145 to 282 mM for PPA. These results demonstrated the potential activity of simple
and non-glycosidic triazoles as an important novel class of GIs for the development of drugs to treat Type
2 DM. | en |
Affilliation | Universidade Federal Fluminense. Instituto de Química. Departamento de Química Orgânica. Niterói, RJ, Brasil. | pt_BR |
Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Bioquímica de Proteínas e Peptídeos. RJ, Brasil | pt_BR |
Affilliation | Universidade Federal Fluminense. Instituto de Química. Departamento de Química Orgânica. Niterói, RJ, Brasil. | pt_BR |
Affilliation | Universidade Federal Fluminense. Instituto de Química. Departamento de Química Orgânica. Niterói, RJ, Brasil. | pt_BR |
Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Bioquímica de Proteínas e Peptídeos. RJ, Brasil | pt_BR |
Subject | Amylase | en |
Subject | Diabetes | en |
Subject | Drug design | en |
Subject | Maltase | en |
Subject | Triazole | en |
Subject | Glycosidase inhibitors | en |