Disruption of bacterial cell wall and membrane integrity by antimicrobial peptide

Antimicrobial peptides (AMPs) are short, often cationic peptides produced by various organisms as part of innate immunity. Their primary antibacterial mechanism is disruption of bacterial cell membrane or wall integrity, leading to leakage of cellular contents and bacterial death. This can proceed via several models, including membrane pore formation (barrel-stave or toroidal pores) or surface-disrupting "carpet" or "detergent-like" mechanisms. AMPs may also bind to specific cell wall molecules (like lipid II) in some bacteria, interfering with cell wall synthesis in addition to membrane disruption. Drugs in this class include naturally derived peptides (melittin, polymyxin B, nisin, gallidermin, mutacin 1140) and engineered AMPs (PepD2M). While AMPs display broad-spectrum antibacterial activity and a lower risk of classical resistance, clinical challenges include possible cytotoxicity to host cells and incomplete specificity for bacterial membranes.

Other names

Antimicrobial peptide-induced membrane disruptionBacterial cell membrane permeabilization by AMPsAMP-mediated bacterial membrane lysis

Membrane pore formation (barrel-stave, toroidal) Surface acting (carpet, detergent-like) Increased membrane permeability leading to osmotic lysis