In eukaryotes, antimicrobial peptides (AMPs) are produced as a part of the innate immune response. AMPs have a broad range of antimicrobial activities, which defend the host organism against bacteria, viruses, and other microbes and serve as a promising substitute for antibiotics in the face of an increasing number of antibiotic resistant bacteria. Novel, designed AMPs can be synthesized as hybrids, in which two AMPs are linked by an amino acid residue. Previous studies have noted that some hybrid AMPs have increased antimicrobial activity and reduced cytotoxicity against eukaryotic cells. This study will focus on two translocating hybrid peptides which are based on the two histone-derived antimicrobial peptides (HDAPs). One is the naturally occurring peptide buforin II (BF2), and the other is the synthesized peptide DesHDAP1. Previous work by the Elmore laboratory has shown that hybrids of BF2 and DesHDAP1 linked by a proline residue display an increase in activity. We designed several variants of this hybrid, such as those including alanine, glycine, and N-methyl alanine linkers, to identify which structural feature of proline promoted this increase in activity. The activity of these hybrid variants have been measured against both bacteria and eukaryotic cells. Circular dichroism (CD) spectroscopy was also used to investigate the relationship between these activity trends and secondary structure. Ongoing work is investigating how linkers affect the membrane interactions of hybrids using confocal microscopy and membrane permeabilization assays.

Investigating how proline linkers enhance antimicrobial peptide hybrid activity

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.