Dye-release assay for investigation of antimicrobial peptide activity in a competitive lipid environment
AuthorSani, M-A; Gagne, E; Gehman, JD; Whitwell, TC; Separovic, F
Source TitleEUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS
University of Melbourne Author/sGEHMAN, JOHN; Sani, Marc Antoine; Separovic, Frances; GAGNE, EVE; WHITWELL, THOMAS
AffiliationBusiness & Economics
School of Chemistry
Document TypeJournal Article
CitationsSani, M-A; Gagne, E; Gehman, JD; Whitwell, TC; Separovic, F, Dye-release assay for investigation of antimicrobial peptide activity in a competitive lipid environment, EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS, 2014, 43 (8-9), pp. 445 - 450
Access StatusOpen Access
NHMRC Grant codeNHMRC/1008106
Full text Embargoed until: 2015-09-30
A dye-release method for investigating the effect of a competitive lipid environment on the activity of two membrane-disrupting antimicrobial peptides (AMP), maculatin 1.1 and aurein 1.2, is presented. The results support the general conclusion that AMP have greater affinity for negatively charged membranes, for example bacterial membranes, than for the neutral membrane surface found in eukaryotic cells, but only within a competitive lipid environment. Indeed, in a single-model membrane environment, both peptides were more potent against neutral vesicles than against charged vesicles. The approach was also used to investigate the effect of pre-incubating the peptides in a neutral lipid environment then introducing charged lipid vesicles. Maculatin was shown to migrate from the neutral lipid bilayers, where pores had already formed, to the charged membrane bilayers. This result was also observed for charged-to-charged bilayers but, interestingly, not for neutral-to-neutral lipid interfaces. Aurein was able to migrate from either lipid environment, indicating weaker binding to lipid membranes, and a different molecular mechanism for lysis of lipid bilayers. Competitive lipid environments could be used to assess other critical conditions that modulate the activity of membrane peptides or proteins.
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