ArticleFrontiers in cellular and infection microbiology2025
Bovine lactoferricin exerts antibacterial activity against four Gram-negative pathogenic bacteria by transforming its molecular structure.
Article in Frontiers in cellular and infection microbiology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Review
- Dairy Bioactive Compounds as Precision Modulators of Gut Microbiota: From Molecular Mechanisms to Personalized Immunometabolic Health.Foods (Basel, Switzerland) · 2026Review
- Bioactive Peptides from Bovine Colostrum: Sources, Structures, and Biomedical Applications.Probiotics and antimicrobial proteins · 2026Review
- Antimicrobial peptides and proteins as rheostats of intestinal homeostasis and immunity.Current opinion in immunology · 2026Review
- Natural and Synthetic Peptides as Alternatives to Antibiotics in Intestinal Infections-A Review.Antibiotics (Basel, Switzerland) · 2026Review
- Conformational plasticity and truncational effects on bovine lactoferricin: structural determinants of enhanced antimicrobial activity.Frontiers in cellular and infection microbiology · 2026Article
- Antimicrobial peptides for anticancer and antiviral therapy: last promising update.Discover oncology · 2025Review
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Authors and funding
7 authors.
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Abstract
The emergence and development of pathogenic bacterial resistance to antibiotics pose significant challenges to human health. Antimicrobial peptides (AMPs) are considered promising alternatives to conventional antibiotics. Lactoferricin (Lfcin), a cationic AMP located in the N-terminal region of lactoferrin, serves as the antimicrobial active center of the intact protein. The presence of two cysteines in Lfcin allows for the formation of an intramolecular disulfide bond, which may influence its molecular structure and antibacterial function. To investigate this hypothesis, we synthesized, purified, and identified bovine Lfcin along with two derivatives: Lfcin with a disulfide bond (Lfcin DB) and a mutated form that cannot form the disulfide bond (Lfcin C36G). We analyzed the circular dichroism spectra of these peptides under varying ionic and hydrophobic conditions, while their tertiary structures were predicted using AlphaFold3. Results indicated that increased ionic strength reduced the random coil ratios across all peptides. The secondary structure of Lfcin showed similar percentages with Lfcin C36G in the H
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