Antioxidant Peptides

A special issue of Antioxidants (ISSN 2076-3921). This special issue belongs to the section "Natural and Synthetic Antioxidants".

Deadline for manuscript submissions: 30 October 2025 | Viewed by 1971

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Research Center in Morphology and Applied Immunology, Faculty of Medicine, University of Brasilia, Brasilia 70910-900, Brazil
Interests: animal ecophysiology; antioxidant; biochemical adaptation; comparative physiology; diapause; estivation; free radical; glutathione; oxidative stress; reactive oxygen species; redox biology
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Special Issue Information

Dear Colleagues,

Antioxidant peptides have attracted growing scientific interest for their promising potential as constituents of functional foods and nutraceuticals due to their expected roles in disease prevention and treatment. Antioxidant peptides can be derived from natural proteins through enzymatic hydrolysis or fermentation. Moreover, they can also be found as peptides from natural sources, such as the skin secretions of amphibians, which are rich in peptides that have antioxidant properties. These bioactive molecules exert a range of antioxidant mechanisms, including free radical scavenging, metal ion chelation, and the inhibition of lipid peroxidation. Despite their beneficial biological activities, challenges remain regarding their in vivo stability and bioavailability. Nevertheless, antioxidant peptides are generally appreciated for their low toxicity and the many possibilities they offer for formulation in both food and pharmaceutical applications.

This Special Issue invites original research articles and comprehensive reviews on the identification, characterization, and functional application of antioxidant peptides. Topics of interest include but are not limited to the following:

  • Structure–activity relationships;
  • Novel natural or synthetic sources;
  • Advanced delivery systems;
  • Roles in preventing or alleviating oxidative stress-related diseases.

By assembling current advances in this dynamic field, this issue aims to promote innovation and deepen our understanding of antioxidant peptides in the context of health and nutrition.

Dr. Daniel Carneiro Moreira
Dr. José Roberto de Souza de Almeida Leite
Guest Editors

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Keywords

  • structure–activity relationships
  • novel natural or synthetic sources
  • advanced delivery systems
  • roles in preventing or alleviating oxidative stress-related diseases.

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Published Papers (3 papers)

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Research

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16 pages, 4594 KB  
Article
Discovery of Deer Antler-Derived Antioxidant Peptides Through Computational and Cell-Based Approaches
by Yongxin Jiang, Jingxian Zheng, Yan Zhang, Yuyang Liu, Linlin Zeng and Weiwei Han
Antioxidants 2025, 14(10), 1169; https://doi.org/10.3390/antiox14101169 - 25 Sep 2025
Abstract
Oxidative stress, caused by excessive free radicals, leads to cellular damage and various diseases. Antioxidant peptides from natural proteins offer potential in alleviating this stress. In this study, antioxidant peptides were identified from deer antler proteins using in silico enzymatic hydrolysis and machine [...] Read more.
Oxidative stress, caused by excessive free radicals, leads to cellular damage and various diseases. Antioxidant peptides from natural proteins offer potential in alleviating this stress. In this study, antioxidant peptides were identified from deer antler proteins using in silico enzymatic hydrolysis and machine learning. Peptides with high prediction scores and non-toxic profiles were selected for evaluation. The antioxidant activities of top candidates, PHPAPTL and VPHGL, were confirmed by radical scavenging assays and their protective effects in HepG2 cells. Molecular dynamics simulations revealed stable binding of these peptides to Keap1, enhancing system stability and reducing residue fluctuations at the ligand-binding interface. Key interactions involved Arg415, Arg483, Arg380, and Ser555. Secondary structure analysis showed peptide binding induced local conformational transitions, notably increasing parallel β-sheet formation near active sites. These findings provide mechanistic insight into their antioxidant effects and support their potential application in functional food development. Full article
(This article belongs to the Special Issue Antioxidant Peptides)
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17 pages, 2585 KB  
Article
Novel Hybrid Peptide DEFB126 (1-39)-TP5 Inhibits LPS-Induced Inflammatory Responses and Oxidative Stress by Neutralizing LPS and Blocking the TLR4/MD2-NFκB Signaling Axis
by Yuan Tang, Xuelian Zhao, Zetao Ding, Junyong Wang, Jing Zhang, Yichen Zhou, Marhaba Ahmat, Hao Wang, Yang Zhu, Baseer Ahmad, Zaheer Abbas, Dayong Si, Rijun Zhang and Xubiao Wei
Antioxidants 2025, 14(9), 1117; https://doi.org/10.3390/antiox14091117 - 14 Sep 2025
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Abstract
Lipopolysaccharide (LPS), an essential structural molecule in the outer membrane of Gram-negative bacteria, is recognized as a principal trigger of inflammatory responses and oxidative stress. Thus, the control and clearance of LPS is essential to inhibit LPS-induced excessive inflammation, oxidative stress, and liver [...] Read more.
Lipopolysaccharide (LPS), an essential structural molecule in the outer membrane of Gram-negative bacteria, is recognized as a principal trigger of inflammatory responses and oxidative stress. Thus, the control and clearance of LPS is essential to inhibit LPS-induced excessive inflammation, oxidative stress, and liver injury. In recent years, some native bioactive peptides, such as human β-defensin 126 (DEFB126) and thymopentin (TP5), have been reported to have inhibitory effects against LPS-induced inflammation and oxidative stress. However, the cytotoxicity, weak stability, and poor biological activity have hindered their practical application and clinical development. The development of novel hybrid peptides is a promising approach for overcoming these problems. In this study, we designed a novel hybrid peptide [DTP, DEFB126 (1-39)-TP5] that combines the active center of DEFB126 and full-length thymopentin (TP5). Compared to the parental peptides, DTP has a longer half-life, lower cytotoxicity, and greater anti-inflammatory and antioxidant activity. The anti-inflammatory and antioxidant effects of DTP were demonstrated in a murine LPS-induced sepsis model, which showed that DTP successfully inhibited the indicators associated with LPS-induced liver injury; decreased the contents of TNF-α, IL-6, and IL-1β; increased the level of glutathione (GSH); and improved the activities of catalase (CAT) and superoxide dismutase (SOD). Furthermore, our study revealed that the anti-inflammatory and antioxidant activities of DTP were associated with LPS neutralization, blockade of LPS binding to the Toll-like receptor 4/myeloid differentiation factor 2 (TLR4/MD-2) complex, reduction in reactive oxygen species content, and inhibition of the activation of the nuclear factor kappa-B (NF-кB) signaling pathway. These results elucidate the structural and functional properties of the peptide DTP, reveal its underlying molecular mechanisms, and shed light on its potential as a multifunctional agent for applications in agriculture, food technology, and clinical therapeutics. Full article
(This article belongs to the Special Issue Antioxidant Peptides)
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Review

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22 pages, 1038 KB  
Review
Bioactivities Derived from Dry-Cured Ham Peptides: A Review
by Noelia Hernández Correas, Andrea M. Liceaga, Adela Abellán, Beatriz Muñoz-Rosique and Luis Tejada
Antioxidants 2025, 14(8), 1011; https://doi.org/10.3390/antiox14081011 - 18 Aug 2025
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Abstract
Dry-cured ham is a traditional food in the Mediterranean diet, which, in addition to its sensory qualities, is a natural source of bioactive peptides generated during the curing process through the action of endogenous enzymes on muscle and sarcoplasmic proteins. These low-molecular-weight peptides [...] Read more.
Dry-cured ham is a traditional food in the Mediterranean diet, which, in addition to its sensory qualities, is a natural source of bioactive peptides generated during the curing process through the action of endogenous enzymes on muscle and sarcoplasmic proteins. These low-molecular-weight peptides have attracted growing interest due to their multiple bioactivities, including antihypertensive, antioxidant, antimicrobial, antidiabetic, and anti-inflammatory effects described in vitro, in vivo, and in preliminary human studies. The identification of specific sequences, such as AAPLAP, KPVAAP, and KAAAAP (ACE inhibitors), SNAAC and GKFNV (antioxidants), RHGYM (antimicrobial), and AEEEYPDL and LGVGG (dipeptidyl peptidase-IV and α-glucosidase inhibitors), has been possible thanks to the use of peptidomics techniques, tandem mass spectrometry, and bioinformatics tools that allow their activity to be characterized, their digestive stability to be predicted, and their bioavailability to be evaluated. This review article summarizes current knowledge on the bioactivities of peptides derived from dry-cured ham, advances in their functional characterization, and challenges associated with their application in functional foods and nutraceuticals, with the aim of providing a comprehensive overview of their potential in health promotion and chronic disease prevention. Full article
(This article belongs to the Special Issue Antioxidant Peptides)
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