Universal cell capture by immobilized antimicrobial peptide plantaricin

• N-terminal domain of Plantaricin-423 is highly capable of cell capture.
• Binding level was L. innocua > E. hirae > S. epidermidis > B. coagulans > E. coli > M. smegmatis.
• Peptide concentration-depended binding levels for L. innocua were determined.
• Immobilized peptide displayed antimicrobial activity against L. innocua.

Plantaricin-423 is a short antimicrobial peptide and displays bactericidal activities against several foodborne pathogens and spoilage Gram positive bacteria. The goal of this study was to investigate the potential of using immobilized plantaricin for capturing microorganisms on glass arrays. The peptide used for immobilization consists of N-terminal domain of Plantaricin-423 with an additional cysteine (Pln-17C) to form disulfide bonds with thiol groups present on silanized slides. Our results showed that Pln-17C is able to capture all six strains that were tested with varying affinities. The cell capture occurred within five minutes of incubation and the binding level was highest for Listeria innocua followed by other Gram positive strains tested. Pln-17C was also able to capture Escherichia coli with lower affinity, but the binding was significantly lower for Mycobacterium smegmatis compared to other strains. In addition, we have observed that immobilized Pln-17C maintained its anti-listerial activity; however, it did not kill E. coli as expected. Our results demonstrate the feasibility of utilizing antimicrobial peptides in biosensors for pathogen detection and for creating antimicrobial surfaces. Moreover, in combination with other peptides, different target species from food-borne pathogens to biodefense agents can be captured on more stable, economic, and robust platforms.

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