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Membrane disruption ability of facially amphiphilic helical peptides
Yvonne R Vandenburg1, Bradley D Smith, Eric Biron
1Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN 46556, USA.
Chemical Communications (Cambridge, England)
|August 29, 2002
Abstract:
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.
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