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Inhibition of α-glucosidase activity by potential peptides derived from fermented spent coffee grounds.
Rochín-Medina, Jesús J; Ramírez-Serrano, Estéphany S; Ramírez, Karina.
Afiliação
  • Rochín-Medina JJ; Laboratorio de Microbiología Molecular y Bioactivos, Tecnológico Nacional de México-Instituto Tecnológico de Culiacán, 80220 Culiacán, Mexico. Electronic address: jesus.rm@culiacan.tecnm.mx.
  • Ramírez-Serrano ES; Laboratorio de Microbiología Molecular y Bioactivos, Tecnológico Nacional de México-Instituto Tecnológico de Culiacán, 80220 Culiacán, Mexico. Electronic address: estephany.rs@culiacan.tecnm.mx.
  • Ramírez K; Laboratorio de Microbiología Molecular y Bioactivos, Tecnológico Nacional de México-Instituto Tecnológico de Culiacán, 80220 Culiacán, Mexico. Electronic address: hilda.rm@culiacan.tecnm.mx.
Food Chem ; 454: 139791, 2024 Oct 01.
Article em En | MEDLINE | ID: mdl-38795616
ABSTRACT
The control of α-glucosidase activity has been associated with managing diabetes. We previously identified three peptides with high bioactive indices derived from protein hydrolysates of fermented spent coffee grounds. In this study, the peptides YGF, GMCC, and RMYRY were synthesized and tested in vitro for their α-glucosidase inhibition activity, complemented by in silico analyses. Two of the three peptides significantly inhibited α-glucosidase activity, with the more efficient peptides being YGF and GMCC (0.42 mg/mL), resulting in decreased enzymatic activity of 95.31% and 89.79%, respectively. These peptides exhibited binding free energies with the α-glucosidase complex of -8.5 and - 6.6 kcal/mol, respectively, through hydrogen bonds and van der Waals interactions with amino acids from the active site. Pharmacokinetic analysis indicated that YGF and GMCC profiles were unrelated to toxicity. These results underscore the importance of focusing on food waste bioprocessing products to expand the range of alternatives that could aid in diabetes treatment.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Peptídeos / Resíduos / Alfa-Glucosidases / Fermentação / Inibidores de Glicosídeo Hidrolases Limite: Animals / Humans Idioma: En Revista: Food Chem Ano de publicação: 2024 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Peptídeos / Resíduos / Alfa-Glucosidases / Fermentação / Inibidores de Glicosídeo Hidrolases Limite: Animals / Humans Idioma: En Revista: Food Chem Ano de publicação: 2024 Tipo de documento: Article
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