Role of lipopolysaccharides and lipoteichoic acids on C-Chrysophsin-1 interactions with model Gram-positive and Gram-negative bacterial membranes.

Antimicrobial peptides (AMPs) are attractive as biomaterial coatings because they have broad spectrum activity against different microbes, with a low likelihood of incurring antimicrobial resistance. Direct action against the bacterial membrane is the most common mechanism of action (MOA) of AMPs, with specific MOAs dependent on membrane composition, peptide concentration, and environmental factors that include temperature. Chrysophsin-1 (CHY1) is a broad spectrum salt-tolerant AMP that is derived from a marine fish.

QCM-D characterization of time-dependence of bacterial adhesion.

Quartz crystal microbalance with dissipation monitoring (QCM-D) is becoming an increasingly popular technique that can be employed as part of experimental and modeling investigations of bacterial adhesion. The usefulness of QCM-D derives from this technique's ability to probe binding and interactions under dynamic conditions, in real time. Bacterial adhesion is an important first step in the formation of biofilms, the control of which is relevant to industries that include shipping, water purification, packaging, and biomedical devices.

Proposed Mechanisms of Tethered Antimicrobial Peptide Chrysophsin-1 as a Function of Tether Length Using QCM-D.

Rising antibiotic resistance has led to a call for the development of alternative antibiotics. Antimicrobial peptides (AMPs) are promising, but their potential has not been fully explored because of toxicity and lack of stability in vivo. Multiple recent studies have focused on surface immobilization of AMPs to maximize antimicrobial activity and stability while mitigating toxicity.