@misc{10481/84486,
year = {2023},
month = {10},
url = {https://hdl.handle.net/10481/84486},
abstract = {Food antidiabetic peptides inhibit the enzymes involved in the regulation of the glycemic index (e.g. a-amylase, a-glucosidase and dipeptidyl peptidase-IV (DPP-IV)). This work reviews the antidiabetic peptide sequences reported in the literature, with activity confirmed by using synthetic peptides, and critically discusses their structural features. Moreover, it provides an overview of the potency of in silico analysis tools to predict the in vitro antidiabetic activity of DPP-IV-inhibitory peptides. In addition, the potential degradation of the most active peptides during digestion was evaluated in silico. Therefore, this work advances our understanding on the structure-activity relationship of antidiabetic peptides and provides new insights on their stability during digestion.},
organization = {MCIN/AEI/10.13039/501100011033: PID2020-114137RB-I00},
publisher = {Elsevier},
keywords = {Antidiabetic peptides},
keywords = {DPP-IV},
keywords = {α-glucosidase},
keywords = {α-amylase},
title = {Activity, structural features and in silico digestion of antidiabetic peptides},
doi = {10.1016/j.fbio.2023.102954},
author = {Berraquero García, Carmen and Rivero Pino, Fernando and Ospina, J. Lizeth and Pérez Gálvez, Antonio Raúl and Espejo Carpio, Francisco Javier and Guadix Escobar, Antonio María and García Moreno, Pedro Jesús and Guadix Escobar, Emilia María},
}