The Efficacy of Cecropin Against Multidrug-Resistant Bacteria Is Linked to the Destabilization of Outer Membrane Structure LPS of Gram-Negative Bacteria.

Abstract

The escalating prevalence of antibiotic-resistant bacteria has emerged as a formidable threat to global health, and the quest for alternative antimicrobial agents is imperative. Cecropins, a class of antimicrobial peptides (AMPs), have garnered attention due to their potent bactericidal properties. This investigation delves into the antibacterial prowess of Cecropin A (CA) and Cecropin AD (CAD), showcasing their robust activity against Gram-negative bacteria, inclusive of multidrug-resistant bacteria. The bactericidal efficacy of CA and CAD is characterized by a dose-responsive paradigm, affirming their potential as therapeutic agents. These peptides exhibit minimal cytotoxicity and hemolytic effects, underscoring their safety profile. Advanced experimentation has elucidated that cecropins could disrupt the outer bacterial membrane, targeting lipid A, a pivotal constituent of the lipopolysaccharides (LPS) in the outer membrane as their antimicrobial bullseye. The affinity of cecropins for LPS and their antimicrobial action underscore the therapeutic potential of these peptides in targeting Gram-negative bacterial infections. These insights accentuate the promise of cecropins as viable "antibiotic substitutes," paving the path for their expanded application in combating antibiotic resistance.