Potential anti-diabetic properties of Merlot grape pomace extract: an in vitro, in silico and in vivo study of α-amylase and α-glucosidase inhibition

• Autor(a) principal: Kato-Schwartz, Camila Gabriel
• Data de Publicação: 2018
• Outros Autores: Corrêa, Rúbia C.G., Lima, Diego de Souza, Sá-Nakanishi, Anacharis B. de, Gonçalves, Geferson A., Seixas, Flávio Augusto Vicente, Haminiuk, Charles Windson Isidoro, Barros, Lillian, Ferreira, Isabel C.F.R., Bracht, Adelar, Peralta, Rosane M.
• Tipo de documento: Artigo
• Idioma: eng
• Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
• Texto Completo: http://hdl.handle.net/10198/23365
• topic: Carbohydrate-hydrolysing enzymes; Diabetes; Docking simulations; Flavonoids; Glycemia control; Polyphenols; Winery by-product

A practical approach to control glycemia in diabetes is to use plant natural products that delay hydrolysis of complex sugars and promote the diminution of the release of glucosyl units into the blood plasma. Polyphenolics have been described as being effective in inhibiting amylases and α-glucosidases. Grape pomace is an important sub product of the wine industry, still rich in many compounds such as polyphenolics. In this context, the purpose of this study was to search for possible effects of a grape pomace extract on salivary and pancreatic α-amylases and α-glucosidase, as well as on intestinal glucose absorption. The Merlot grape pomace extract (MGPE) was prepared using a hydroalcoholic mixture (40% ethanol + 60% water). In vitro inhibition was quantified using potato starch (for amylases) and maltose (for α-glucosidase) as substrates. In vivo inhibition was evaluated by running starch and maltose tolerance tests in rats with or without administration of MGPE. Ranking of the extract compounds for its affinity to the α-amylases was accomplished by computer simulations using three different programs. Both α-amylases, pancreatic and salivary, were inhibited by the MGPE. No inhibition on α-glucosidase, however, was detected. The IC50 values were 90 ± 10 μg/mL and 143 ± 15 μg/mL for salivary and pancreatic amylases, respectively. Kinetically this inhibition showed a complex pattern, with multiple binding of the extract constituents to the enzymes. Furthermore, the in silico docking simulations indicated that several phenolic substances, e.g., peonidin-3-O-acetylglucoside, quercetin-3-O-glucuronide and isorhamnetin-3-O-glucoside, besides catechin, were the most likely polyphenols responsible for the α-amylase inhibition caused by MGPE. The hyperglycemic burst, an usual phenomenon that follows starch administration, was substantially inhibited by the MGPE. Our results suggest that the MGPE can be adequate for maintaining normal blood levels after food ingestion.