Membrane interactions of antimicrobial beta-peptides: the role of amphipathicity versus secondary structure induction.

Kristopher Norman Hall, Marie Isabel Aguilar

Research output: Contribution to journalArticleResearchpeer-review

13 Citations (Scopus)

Abstract

The membrane interaction of two beta peptides was studied using a surface plasmon resonance biosensor. The two peptides are beta-17, a novel I?-amino acid based antimicrobial peptide and the corresponding scrambled-beta17 a?? a non-antimicrobial beta-peptide analogue. Membrane - interaction studies were performed with a series of phospholipid mixtures which mimic either mammalian cells (high in phosphatidylcholine and cholesterol) or microbial cells (high in phosphatidylethanolame and phosphatidylglycerol). The results were compared with the membrane binding of the well-characterised antimicrobial peptide magainin 2. The secondary structure of these peptides were also determined in each lipid mixture by circular dichroism and correlated with the membrane-binding properties. Both beta-17 and the scrambled peptide have the same peptide length, charge and showed a similar secondary structure in both aqueous buffer and in the presence of liposomes. Both peptides also bound to a similar level on each membrane mixture, showing that the dramatic difference in biological activity is not based on the amount of peptide bound but rather differences in the degree of insertion and rate of membrane dissociation. While beta-17 and the scrambled beta-17 peptide exhibited similar binding properties on all membrane mimics, both beta-peptides bound more to all membranes compared to magainin 2. Overall, the results further reveal the significant interplay between peptide amphipathicity and secondary structure induction upon membrane binding.
Original languageEnglish
Pages (from-to)554 - 564
Number of pages11
JournalBiopolymers (Peptide Science)
Volume92
Issue number6
DOIs
Publication statusPublished - 2009

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