TL;DR
Rational peptide engineering can generate stable and potent AMPs with precise membrane-associated targets, as exemplified by CAMP502NC3, which demonstrates potent activity against Staphylococcus aureus and remained stable under diverse conditions.
While the peptide shows promising in vitro dual antibacterial and toxin-neutralizing capacity, its high sensitivity to proteinase K limits oral application.
A site-selective semisynthetic modification strategy via reductive amination of bacitracin A's N-terminal primary amine is established, providing a rational strategy for bacitracin optimization and highlighting the potential of N-terminal modification for developing improved antibacterial agents.
High selectivity for pathogenic strains over mammalian host cells is a fundamental prerequisite for an antimicrobial therapeutic. Hydrophobic–hydrophilic balance has been a cornerstone for modulating AMP performance. Here, we have refined the selectivity of 2BWWR-7dL by modulating the hydrophilic–hydrophobic balance th...
The consensus-sequence approach toward novel Brevinin-2 AMP discovery via alignment combined with in vitro antimicrobial analysis shows promise to test and initially validate other peptides, and establishes a streamlined pipeline for Brevinin-2 peptide development.
The findings suggest that optimizing lipid–peptide combinations can lead to more effective, specific, and stable candidates for antimicrobial development.
The optimized peptide G5P2 exhibits potent antibacterial activity via a typical membrane-disrupting mechanism, is not prone to inducing bacterial drug resistance, can synergize with traditional antibiotics to delay the emergence of antibiotic resistance, and has excellent in vivo antibacterial activity and high safety.
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