ArticleProbiotics and antimicrobial proteins2026
From Bacteria to Breakthroughs: Design and Evaluation of Gallocin-Based Peptide for Colorectal Cancer Therapeutic.
Article in Probiotics and antimicrobial proteins, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Developing targeted cancer therapies with high selectivity, low toxicity, and cost-effectiveness remains a major challenge in modern medicine. This study aimed to design a Gallocin-derived anticancer peptide (ACP) targeting the epidermal growth factor receptor (EGFR) using an integrated bioinformatics and experimental approach. Gallocin, a bacteriocin from Streptococcus gallolyticus, was selected for its unique four α-helix structure and anticancer motifs, making it a promising candidate for ACP in initial in silico analysis. The Gallocin-derived ACPs were predicted using web-based tools. Molecular docking studies assessed the binding affinity of ACPs to EGFR, and molecular dynamics simulations analyzed the stability of the Galcn-1-EGFR complex. The absorption, distribution, metabolism, excretion, and toxicity (ADMET) analysis evaluated pharmacokinetic properties. Docking revealed that Galcn-1 had a high binding affinity for EGFR, forming stable hydrogen bonds. Molecular dynamics simulations confirmed complex stability. Experimental validation showed that Galcn-1 exhibited an IC₅₀ of 16 µg/ml in HT-29 cells. Galcn-1 downregulated EGFR and PI3K expression, induced apoptosis via both extrinsic (CAS-8) and intrinsic (CAS-9) pathways, increased ROS production, and caused cell cycle arrest in the S-phase. Pharmacokinetic evaluations indicated improved metabolism and lower toxicity, along with decreased permeability and a shorter half-life. Future optimization through bioengineering, such as peptide conjugation and chemical modifications (PEGylation), use of a synthetic staple, and development of drug delivery systems, will enhance stability, protect the peptide from proteolytic degradation, extend its half-life and binding affinity, and improve permeability and function, positioning Galcn-1 for further preclinical and clinical development.
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