Membrane disruption ability of facially amphiphilic helical peptides.
A helical 14-residue peptide containing four polar, but uncharged, benzo-21-crown-7 side-chains aligned along one face induces significantly more vesicle leakage than analogous 21-mer or 7-mer peptides.
Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN 46556, USA.
Yvonne R
YR
Vandenburg
Bradley D
BD
Smith
Eric
E
Biron
Normand
N
Voyer
D002463:Cell Membrane Permeability / Q000187:drug effects*; D005452:Fluoresceins / Q000493:pharmacokinetics; D057927:Hydrophobic and Hydrophilic Interactions; D008081:Liposomes; D008954:Models, Biological; D009842:Oligopeptides / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology*; D017433:Protein Structure, Secondary; D013329:Structure-Activity Relationship
D005452:Fluoresceins; D008081:Liposomes; D009842:Oligopeptides; C007740:fluorexon