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Chemoselective surface attachment of antimicrobial peptides and its effects on interfacial behavior

Peptide-based biological recognition elements are valuable tools for detection in biodefense systems. The utilization of such biomolecules for detection purposes relies on the ability to immobilize them on the surface of a detection platform in a predictable and reliable manner that facilitates target binding. Numerous immobilization methods have been used to improve the performance of peptide-based biosensors; however, the molecular details of how surface attachment affects structure and activity require further investigation to establish general approaches for obtaining consistent sensor surfaces. This has been largely due to the lack of analytical techniques. Using surface spectroscopy techniques, we examined the secondary structure of peptides tethered to solid support. Different tethering parameters were investigated by substituting a cysteine residue to the N-terminus or C-terminus in cationic antimicrobial peptides, and its effects on antimicrobial activity against gram-negative bacteria, E. coli. Spectroscopic analysis showed that surface immobilization drives transition of peptides secondary structures, resulting in different interfacial behaviors that may influence the secondary structure of the peptides once they interact with the bacterial cells. We have begun to gain insight into how surface attachment may have direct implications for peptide presentation and function and is an important advance in preparing a robust sensing interface.