Antimicrobial peptides: Antimicrobial peptides (AMPs) are gaining popularity in the treatment of drug-resistant bacteria as alternatives for more traditional small molecule antibiotics. They are mostly bioactive proteins naturally produced by all types of living organisms as host defense system 248 , 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 non-ribosomally synthesized peptides, linear and cyclic peptides, 255 or based on their secondary structure. In general, antimicrobial peptides 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, 259 some examples of them are glycopeptides, lipopeptides, lipoglycopeptides, lantibiotics, 260-267 defensins, 268 and thiopeptides. We will be briefly discussing the first 3 categories, but for more general information on emerging antibiotic peptides, structure-activityrelationships (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. Figure suggests that antimicrobial peptides show a steady growth till 2020 in both journal and patent publications. Interestingly, the growth in patent publications is faster as compared to journal publications, indicating commercial interest in this area. Notable categories of antimicrobial peptides are: Glycopeptides: Glycopeptides are glycosylated non-ribosomal peptides that are composed of tricyclic or tetracyclic polypeptide scaffold, typically a heptapeptide scaffold made by proteogenic and nonproteogenic amino acids alongside sugar residues, chlorine atoms, methyl groups, or lipid chains. They display antibacterial activity against Gram-positive bacteria typically by inhibiting cell wall biosynthesis due to binding to the C-terminal D-Ala-D-Ala moiety of the peptidoglycan precursor Lipid II, preventing transglycosylation and transpeptidation for cell wall synthesis. They are effective against Staphylococcus aureus (including MRSA), Enterococcus spp., Clostridium difficile, and healthcare-associated infections that are resistant to other antibiotics like Enterococcus faecalis and Enterococcus faecium. Some members of approved drugs of this group are Vancomycin (1958), 278 teicoplanin (1988), 279 telavancin (2009), 280 dalbavancin (2014), 281 oritavancin (2014). Many novel derivatives and new glycopeptides are also being developed, studied, and optimized. Known resistance mechanisms include target site modification, cell wall thickening, enzymatic modification of vancomycin and efflux pumps. 284