Binding of cationic model peptides (KX)₄K to anionic lipid bilayers: Lipid headgroup size influences secondary structure of bound peptides

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• 作者：André ; Hä ; dicke ; Alfred Blume ; ^{alfred.blume@chemie.uni-halle.de}
• 关键词：Cationic peptides ; Anionic lipids ; Hydrophobic interaction ; Electrostatic interaction ; Differential scanning calorimetry ; FT-IR-spectroscopy
• 刊名：Biochimica et Biophysica Acta (BBA) - Biomembranes
• 出版年：2017
• 出版时间：March 2017
• 年：2017
• 卷：1859
• 期：3
• 页码：415-424
• 全文大小：1363 K
• 卷排序：1859

文摘

Binding of peptides (KX)4K to PS, PG, PA, and CL membranes was studied by DSC and FT-IR. Hydrophobicity of X and size of lipid headgroup determines secondary structure when membrane-bound. The secondary structure of (KX)4K can change with temperature. For PS membranes bound β − sheets are transformed to unordered structures above Tm. β − sheets are stable even above Tm when bound to PA and CL membranes.