“…They are mostly bioactive proteins naturally produced by all types of living organisms as a host defense system, though some artificial AMPs have also been synthesized . AMPs are typically short (<100 amino acids) amphiphilic cationic peptides with a broad spectrum of antimicrobial activity, an overall net charge of +2 to +11 with around 50% of hydrophobic residues, many positive residues (arginine, lysine, histidine), and a molecular weight of <10kD. ,− They can be divided into many ways: ribosomally synthesized peptides and nonribosomally synthesized peptides, , linear and cyclic peptides, or on the basis of their secondary structure. , In general, AMPs target the cell membranes of pathogens; more details on their mechanisms of actions can be found in reviews by Moretta et al, Zhu et al, and Zhang et al There are over 3000 natural AMPs as of November 2022 according to the Antimicrobial Peptide Database; some examples of them are glycopeptides, lipopeptides, lipoglycopeptides, lantibiotics, − defensins, and thiopeptides. − We will be briefly discussing the first three categories, but for more general information on emerging antibiotic peptides, structure–activity relationship (SAR) studies, strategies to improve AMP activity and biocompatibility, AMP applications, resistance, AMPs in clinical trials, etc., please refer to previous reviews cited in this paragraph. Self-assembled peptide nanomaterials are used to inhibit bacterial growth …”