1. Blake, K. L. & O’Neill, A. J. Transposon library screening for identification of genetic loci participating in intrinsic susceptibility and acquired resistance to antistaphylococcal agents. J. Antimicrob. Chemother. 68, 12–16 (2013).
2. Hancock, R. E. W. Peptide antibiotics. Lancet 349, 418–422 (1997).
3. Mookherjee, N. & Hancock, R. E. W. Cationic host defence peptides: innate immune regulatory peptides as a novel approach for treating infections. Cell. Mol. Life Sci. 64, 922–933 (2007).
4. Schwessinger, B. & Zipfel, C. News from the frontline: recent insights into PAMP-triggered immunity in plants. Curr. Opin. Plant Biol. 11, 389–395 (2008).
5. Chaudhary, S., Ali, Z. & Mahfouz, M. Molecular farming for sustainable production of clinical-grade antimicrobial peptides. Plant Biotechnol. J. 22, 2282–2300 (2024).
6. De Breij, A. et al. The antimicrobial peptide SAAP-148 combats drug-resistant bacteria and biofilms. Sci. Transl Med. 10, eaan4044 (2018). This study identifies SAAP-148 as a promising AMP capable of eradicating multidrug-resistant bacteria, biofilms and persister cells, with minimal resistance potential, paving the way for innovative treatments against antibiotic-resistant infections.
7. Bacalum, M. & Radu, M. Cationic antimicrobial peptides cytotoxicity on mammalian cells: an analysis using therapeutic index integrative concept. Int. J. Pept. Res. Ther. 21, 47–55 (2015).
8. Brown, P. & Dawson, M. J. Development of new polymyxin derivatives for multi-drug resistant Gram-negative infections. J. Antibiot. 70, 386–394 (2017).
9. Hancock, R. E. W. & Lehrer, R. Cationic peptides: a new source of antibiotics. Trends Biotechnol. 16, 82–88 (1998).
10. Zasloff, M. Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor. Proc. Natl Acad. Sci. USA 84, 5449–5453 (1987).
11. Mandard, N., Bulet, P., Caille, A., Daffre, S. & Vovelle, F. The solution structure of gomesin, an antimicrobial cysteine-rich peptide from the spider. Eur. J. Biochem. 269, 1190–1198 (2002).
12. Selsted, M. E. et al. Indolicidin, a novel bactericidal tridecapeptide amide from neutrophils. J. Biol. Chem. 267, 4292–4295 (1992).
13. Tang, Y. Q. et al. A cyclic antimicrobial peptide produced in primate leukocytes by the ligation of two truncated α-defensins. Science 286, 498–502 (1999).
14. Craik, D. J., Daly, N. L., Bond, T. & Waine, C. Plant cyclotides: a unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif. J. Mol. Biol. 294, 1327–1336 (1999).
15. Sneideris, T. et al. Targeting nucleic acid phase transitions as a mechanism of action for antimicrobial peptides. Nat. Commun. 14, 7170 (2023). This article reveals that AMPs can induce phase transitions in bacterial nucleic acids, providing a novel mechanism for their antibacterial activity.
16. Seefeldt, A. C. et al. Structure of the mammalian antimicrobial peptide Bac7(1–16) bound within the exit tunnel of a bacterial ribosome. Nucleic Acids Res. 44, 2429–2438 (2016).
17. Ghosh, A. et al. Indolicidin targets duplex DNA: structural and mechanistic insight through a combination of spectroscopy and microscopy. Chem. Med. Chem. 9, 2052–2058 (2014).
18. Koehbach, J. & Craik, D. J. The vast structural diversity of antimicrobial peptides. Trends Pharmacol. Sci. 40, 517–528 (2019).
19. Hsu, C. H. et al. Structural and DNA-binding studies on the bovine antimicrobial peptide, indolicidin: evidence for multiple conformations involved in binding to membranes and DNA. Nucleic Acids Res. 33, 4053–4064 (2005).
