| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10798007 | Biochimica et Biophysica Acta (BBA) - Biomembranes | 2011 | 9 Pages |
Abstract
âºEffects of different hydrophobic modifications in CNY21 antimicrobial peptide were investigated by NMR and ellipsometry. âºBoth hydrophobic modifications promote peptide binding to membranes, membrane disruption, and bacterial killing. âºCNY21L penetrates into the membrane interior in the absence of cholesterol, but is unable to do so in the presence of cholesterol. âºCNY21WWW displays relatively shallow localization in the membrane irrespective of cholesterol, but is not excluded from the membrane by cholesterol.
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Authors
Greger Orädd, Artur Schmidtchen, Martin Malmsten,