Integrated proteomics and in silico analysis of casein-derived peptides with antioxidant, antihypertensive, and anticancer activities
Year: 2025
Type: article
Abstract: Bioactive peptides (BAPs) from milk proteins hold promise for functional foods and therapeutics due to their diverse biological activities and low toxicity. This study identified novel casein-derived peptides using simulated gastrointestinal digestion, proteomics, and in-silico prediction tools. High-resolution tandem mass spectrometry and computational screening led to the identification of three novel peptides: FVAPFPEVFG (αCN) , NLLRF (αCN) , and EMPFPKY (βCN) . Chemical and cellular assessments revealed distinct bioactive profiles, with EMPFPKY (βCN) demonstrating superior antioxidant activity through Keap1 binding, while FVAPFPEVFG (αCN) exhibited dual ACE-inhibitory and anticancer properties against MCF-7 breast cancer cells. Furthermore, the selective cytotoxicity of NLLRF (αCN) against MCF-7 cancer cells, while preserving the viability of normal cells, suggested its potential for therapeutic applications. This comprehensive approach, combining experimental and computational methods, establishes a robust pipeline for identifying and characterizing bioactive peptides, contributing to the development of novel functional food products and pharmaceutical applications. • Novel milk peptides identified with distinct functional bioactivities. • EMPFPKY (β-CN) reduces oxidative stress via Nrf2-linked radical scavenging. • FVAPFPEVFG (α-CN) shows ACE inhibition with strong binding affinity. • NLLRF (α-CN) and FVAPFPEVFG (α-CN) target MCF-7 cells sparing normal cells. • Computational and experimental integration streamlines peptide discovery.
Source: Food Chemistry
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: hybrid
Estimated APC paid: $4,930
OpenAlex ID: W4413203523