Antioxidant Peptides in Focus: A Structural and Predictive Analysis of Radical Scavenging Mechanisms

Antioxidant peptides are crucial biomolecules that effectively neutralize reactive oxygen species and protect against oxidative damage. In this study, an extensive set of short peptides was initially screened to identify potential antioxidant candidates, from which five top-ranking peptides were selected for in-depth computational analysis. Utilizing advanced structural prediction and visualization tools such as AlphaFold, PyMOL, and Chimera, these peptides were characterized to assess their solvent-accessible surface area (SASA), the spatial arrangement of key antioxidant residues-including cysteine, methionine, tyrosine, tryptophan, and histidine-and their predicted bioactivity. Among them, peptides AP02260 and AP03569 were predicted to possess higher antioxidant potential, supported by elevated SASA values and strong predicted free radical scavenging (FRS) and metal chelation (CHEL) scores generated by machine-learning models. Notably, structural analysis of AP03569 revealed a putative semi-compact antioxidant core composed of two alpha-helices linked by a central loop, which may facilitate optimal interactions among critical residues involved in radical neutralization. These computational findings provide structural hypotheses regarding peptide antioxidant activity and identify promising candidates for future experimental validation and potential therapeutic development.

Dergi

INTERNATIONAL JOURNAL OF PEPTIDE RESEARCH AND THERAPEUTICS

Yıl

2025

Cilt

32

Sayı

1

ISSN

1573-3149

eISSN

1573-3904

DOI

10.1007/s10989-025-10780-5

WoS UID

WOS:001626403400001