Antimicrobial action and mechanism of piscidin against Helicobacter pylori

The rise of antibiotic-resistant Helicobacter pylori (Hp) strains is complicating the management of common gastrointestinal conditions such as gastritis and ulcers. In search of effective treatment options, antimicrobial peptides are being explored as a promising strategy.

Leveraging bioinformatics, we dissected structural and sequence profiles of piscidin, an antimicrobial peptide. We investigated whether long-term piscidin exposure induces resistance in Hp strains by measuring their minimum inhibitory concentration. The Oxford cup test was applied to measure inhibition zones of piscidin against Hp strains. Following piscidin treatment, we monitored morphological alterations in Hp strains using scanning electron microscopy, and changes in urease activity, expressions of virulence factors CagA and UreB, and adenosine triphosphate levels. Cytotoxicity of piscidin was evaluated in AGS and 293T cells.

Piscidin inhibited proliferation of Hp strains, with a low propensity of inducing resistance. Delving into underlying mechanisms, we observed piscidin could alter morphology of Hp strains, suppress urease activity, and downregulate expressions of virulence factors CagA and UreB, while also reducing intracellular ATP levels. Piscidin had good security.

Piscidin is a potent antibacterial agent against Hp with low resistance risk, making it a safe and effective treatment candidate.