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.
Highlights
Bioactive peptides have been an important subject of research in recent years due to their wide range of bioactivities [1] and have been proposed as alternative, preventive, and therapeutic agents against diverse diseases, including cancer [2]
The aim of this study is to predict and analyze α-zein derived peptides using in silico tools and to evaluate their cytotoxicity, cell-penetrating ability and antioxidant and angiotensin-converting enzyme (ACE) inhibitory activities in vitro
Our results indicated that the experimental peptides had only low cell-penetrating activity in both cell lines compared to standards
Summary
Bioactive peptides have been an important subject of research in recent years due to their wide range of bioactivities [1] and have been proposed as alternative, preventive, and therapeutic agents against diverse diseases, including cancer [2]. One of the most studied features of bioactive peptides is their capacity to penetrate the cell, named cell-penetrating peptides (CPPs) [5]. This class of peptides can pass through cell membranes and exert their bioactivity inside the cell or act as carriers for other molecules, such as proteins, peptides, lipids, antibiotics, and drugs [6]. Antihypertensive effects have been suggested, as some peptides can inhibit angiotensin-converting enzyme (ACE) [8]. ACE is one of the main enzymes of the renin–angiotensin–aldosterone system and is responsible for the cleavage of angiotensin I to angiotensin II, which has a key role in the pathogenesis of hypertension [9]
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