Activity, structural features and in silico digestion of antidiabetic peptides Berraquero García, Carmen Rivero Pino, Fernando Ospina, J. Lizeth Pérez Gálvez, Antonio Raúl Espejo Carpio, Francisco Javier Guadix Escobar, Antonio María García Moreno, Pedro Jesús Guadix Escobar, Emilia María Antidiabetic peptides DPP-IV α-glucosidase α-amylase Funding This research was funded by the grant PID2020-114137RB-I00 funded by MCIN/AEI/10.13039/501100011033 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. 2023-09-19T07:05:11Z 2023-09-19T07:05:11Z 2023-10 journal article C. Berraquero-García et al. Activity, structural features and in silico digestion of antidiabetic peptides. Food Bioscience 55 (2023) 102954. [https://doi.org/10.1016/j.fbio.2023.102954] https://hdl.handle.net/10481/84486 10.1016/j.fbio.2023.102954 eng http://creativecommons.org/licenses/by-nc-nd/4.0/ open access Attribution-NonCommercial-NoDerivatives 4.0 Internacional Elsevier