ArticleFrontiers in microbiology2022
Optimization of Antibacterial Activity in Tibetan Swine α-Helix Peptide TP by Site-Directed Mutagenesis.
Article in Frontiers in microbiology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed, 6 citations in OpenAlex.
- Functional Peptides: Comparing Synthetic and Sequence-Engineered Antibiofilm Pharmaceutics.Pharmaceutics · 2026Review
- Recombinant Expression and Antimicrobial Mechanism of Cysteine-Rich Antimicrobial Peptides fromMarine drugs · 2026Article
- Advances of Antimicrobial Peptide-Based Biomaterials for the Treatment of Bacterial Infections.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Review
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Authors and funding
8 authors at 1 institution in 1 country.
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Abstract
Antimicrobial peptides (AMPs) have attracted extensive attention because of their broad-spectrum antibacterial activity and low level of induced bacterial resistance. However, the development of some natural AMPs does not consider the perfect balance of structural characteristics, resulting in some empirical and controversial practices still existing. To further explore and complete the relationship between parameters and function of α-helix peptide, in this study, the natural antimicrobial peptide TP secreted from Bacillus strain of Tibetan pigs was selected as a template to investigate the effect of systematic mutations in the hydrogen bond formation site of the α-helical antimicrobial peptide on the activity and cell selectivity of the antimicrobial peptide. The target peptide TP(i+4) 1&2&5 with modification of two pairs of positively charged amino acids and a pair of hydrophobic amino acids showed excellent antibacterial ability and the best selectivity index (SI = 64)
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