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The Activity of the Amphipathic Peptide δ-Lysin Correlates with Phospholipid Acyl Chain Structure and Bilayer Elastic Properties

Release of lipid vesicle content induced by the amphipathic peptide δ-lysin was investigated as a function of lipid acyl chain length and degree of unsaturation for a series of phosphatidylcholines. Dye efflux and peptide binding were examined for three homologous lipid series: di-monounsaturated, d...

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Bibliografische gegevens
Hoofdauteurs: Pokorny, Antje, Kilelee, Erin M., Wu, Diana, Almeida, Paulo F. F.
Formaat: Artigo
Taal:Inglês
Gepubliceerd in: The Biophysical Society 2008
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Online toegang:https://ncbi.nlm.nih.gov/pmc/articles/PMC2576357/
https://ncbi.nlm.nih.gov/pubmed/18708459
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1529/biophysj.108.138701
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