ArticleMolecules (Basel, Switzerland)2020
In Silico Analysis and In Vitro Characterization of the Bioactive Profile of Three Novel Peptides Identified from 19 kDa α-Zein Sequences of Maize.
Article in Molecules (Basel, Switzerland), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 25 citations in OpenAlex.
- Antioxidant, Hypotensive, and Antidiabetic Breakthroughs: Bromelain Hydrolysis Unlocks Quinoa's Peptide Potential -Journal of agricultural and food chemistry · 2025Article
- Molecular Modelling in Bioactive Peptide Discovery and Characterisation.Biomolecules · 2025Review
- Bioactive Peptides from Corn (Biology · 2024Review
- Shifting archetype to nature's hidden gems: from sources, purification to uncover the nutritional potential of bioactive peptides.3 Biotech · 2023Review
- Identification of Bioactive Peptides from aMarine drugs · 2023Article
- An integrated approach to the analysis of antioxidative peptides derived from Gouda cheese with a modified β-casein content.Scientific reports · 2022Article
- Conventional andFood chemistry: X · 2022Article
- Cocoa (Foods (Basel, Switzerland) · 2021Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
In this study, we characterized three novel peptides derived from the 19 kDa α-zein, and determined their bioactive profile in vitro and developed a structural model in silico. The peptides, 19ZP1, 19ZP2 and 19ZP3, formed α-helical structures and had positive and negative electrostatic potential surfaces (range of -1 to +1). According to the in silico algorithms, the peptides displayed low probabilities for cytotoxicity (≤0.05%), cell penetration (10-33%) and antioxidant activities (9-12.5%). Instead, they displayed a 40% probability for angiotensin-converting enzyme (ACE) inhibitory activity. For in vitro characterization, peptides were synthesized by solid phase synthesis and tested accordingly. We assumed α-helical structures for 19ZP1 and 19ZP2 under hydrophobic conditions. The peptides displayed antioxidant activity and ACE-inhibitory activity, with 19ZP1 being the most active. Our results highlight that the 19 kDa α-zein sequences could be explored as a source of bioactive peptides, and indicate that in silico approaches are useful to predict peptide bioactivities, but more structural analysis is necessary to obtain more accurate data.
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