Development of antimicrobial resistance in commonly occurring pathogens renders the existing microbicidal agents including conventional antibiotics largely ineffective. This problem is further complicated by the ease of biofilm formation, particularly on implantable biomedical devices. Much effort on alternative antimicrobial strategies is underway, including the use of antimicrobial peptides (AMPs), which are advantaged by their broad spectrum activity and reduced likelihood to incur pathogen resistance due to their mechanism of action which targets parts of the pathogens that are hard to evolve. As such, their potential as coating material for implantable bio-devices to prevent consequent infections is very promising. However, peptide immobilization strategies that will retain peptide structural integrity, broad antimicrobial activity and salt tolerance remain a key challenge for the successful use of AMPs as an antimicrobial coating agent. This study reports the successful development of biochemical strategies to immobilize short cysteine-linked AMP candidates on biocompatible materials functionalized with optimized bi-functional cross linkers that can facilitate AMP immobilization whilst retaining their activity. Detailed structure-function characterization studies of the immobilized peptides showed that tethering did not compromise AMP antimicrobial potency and induced swift killing of pathogens coming in contact with the surface was observed using the same mechanism of action as their soluble peptide counterparts. The successful extension of this immobilization platform on biomedically relevant surfaces such as catheters now opens the way for the development of biocompatible and infection-resistant catheters, which are long term solutions to addresss catheter-associated infections.

Tethering short antimicrobial peptides on biomedical relevant surfaces: Structure-function studies

245th National Meeting (2013)

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