| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10797851 | Biochimica et Biophysica Acta (BBA) - Biomembranes | 2011 | 7 Pages |
Abstract
⺠Tat peptides disrupt bacterial-mimetic membranes via surface-active mechanisms. ⺠Peptide binding increases with greater negatively charged lipid composition. ⺠Membrane disruption decreases with increasing negative membrane charge. ⺠Membrane disruption less for Tat (44-57) compared with Tat (49-57). ⺠Both Tat peptides bind to mammalian-mimetic membranes without disruption.
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Authors
Stefania Piantavigna, George A. McCubbin, Solveig Boehnke, Bim Graham, Leone Spiccia, Lisandra L. Martin,