Hipposin is a histone H2A derived antimicrobial peptide that contains two proline residues. Recently we compared the structure, antimicrobial activity and membrane permeabilizing ability of hipposin and mutant forms converting proline to alanine. Circular dichroism spectroscopy showed that hipposin and its mutants are primarily a-helical. Cellular permeabilization assays with propidium iodide demonstrated that single proline mutants increased the membrane permeabilizing ability of the peptide. Interestingly, these permeabilization results did not fully correlate with the antimicrobial activity of the peptides against various bacterial strains. Ongoing studies are considering the ability of hipposin and its proline variants to translocate across cell membranes.

Investigating the mechanism of the histone H2A derived antimicrobial peptide hipposin

243rd National Meeting (2012)

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