Journal
FOOD RESEARCH INTERNATIONAL
Volume 150, Issue -, Pages -Publisher
ELSEVIER
DOI: 10.1016/j.foodres.2021.110753
Keywords
Bioactive peptides; Top-down approach; angiotensin I converting enzyme; In silico screening; Egg proteins
Categories
Funding
- project Mime4Health [986/2018 PORFESR_2014_2020]
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Bioactive peptides are short peptides with specific biological activities, crucial for understanding the physiological consequences of food and designing novel food products. The identification of bioactive peptides is challenging and mainly relies on bottom-up approaches. A top-down, computer-assisted and hypothesis-driven method was presented to identify potent angiotensin I converting enzyme inhibitory tripeptides, showing promising results for high-throughput identification of bioactive peptides.
Bioactive peptides are short peptides (3-20 amino acid residues in length) endowed of specific biological activities. The identification and characterization of bioactive peptides of food origin are crucial to better understand the physiological consequences of food, as well as to design novel foods, ingredients, supplements, and diets to counteract mild metabolic disorders. For this reason, the identification of bioactive peptides is also relevant from a pharmaceutical standpoint. Nevertheless, the systematic identification of bioactive sequences of food origin is still challenging and relies mainly on the so defined bottom-up approaches, which rarely results in the total identification of most active sequences. Conversely, top-down approaches aim at identifying bioactive sequences with certain features and may be more suitable for the precise identification of very potent bioactive peptides. In this context, this work presents a top-down, computer-assisted and hypothesis-driven identification of potent angiotensin I converting enzyme inhibitory tripeptides, as a proof of principle. A virtual library of 6840 tripeptides was screened in silico to identify potential highly potent inhibitory peptides. Then, computational results were confirmed experimentally and a very potent novel sequence, LMP was identified. LMP showed an IC50 of 15.8 and 6.8 mu M in cell-free and cell-based assays, respectively. In addition, a bioinformatics approach was used to search potential food sources of LMP. Yolk proteins were identified as a possible relevant source to analyze in further experiments. Overall, the method presented may represent a powerful and versatile framework for a systematic, high-throughput and top-down identification of bioactive peptides.
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