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Exploring vesicle size as a variable in antimicrobial peptide‐lipid vesicle interactions
Author(s) -
Shortt Emily M.,
Elmore Donald E.
Publication year - 2013
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.27.1_supplement.587.2
Subject(s) - magainin , vesicle , antimicrobial peptides , membrane , membrane curvature , biology , peptide , biochemistry , lipid bilayer , chemistry , biophysics , microbiology and biotechnology
Antimicrobial peptides (AMPs) selectively kill bacteria, fungi, and some cancer cells, either by membrane permeabilization or by translocation across the membrane and interference with intracellular processes. Lipid vesicles provide an effective model of cell membranes that can be prepared in various sizes to examine the effect of local membrane curvature on AMP activity. Magainin and buforin II are well‐characterized permeabilizing and translocating peptides, respectively, and DesHDAP1, DesHDAP3, and DesHDAP3 P13A are designed histone‐derived peptides that are translocating (DesHDAP1) or permeabilizing (DesHDAP3 and DesHDAP3 P13A). We performed fluorescence assays to measure the membrane permeabilization and translocation of these peptides with different sized lipid vesicles. Magainin and DesHDAP3 P13A permeabilized smaller vesicles more effectively than large ones. Buforin II and DesHDAP1 translocated more readily with increasing vesicle size. We also found that DesHDAP3 showed translocating activity with larger vesicles but not smaller vesicles, highlighting the potential effect of membrane curvature on antimicrobial mechanisms.