Antimicrobial peptides are a class of small (&lt;100 aa) polypeptides that are secreted by many organisms as a form of protection. They are of considerable interest due to their potential for use against bacteria that are resistant to traditional antibiotics. Most cationic antimicrobial peptides are thought to cause cell death by aggregating on the surface of the bacterial membrane, forming pores or otherwise disrupting membrane integrity. We are investigating whether dimerization to pre-organize antimicrobial peptides can increase their activity against bacteria, and whether linker length or peptide orientation have any effect on this activity. Homodimers of two antimicrobial peptides, parasin I and buforin II, have been prepared using maleimide-thiol conjugation. The activity of the dimers is similar to the activity of the unlinked, unmodified peptide. However, our results show that the modifications required for dimerization decrease the efficacy of the peptide in some cases; the activity is then recovered upon dimerization.

Effect of dimerization on the activity of two antimicrobial peptides

2019 Spring National Meeting

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