@article{Kleinschmidt1997Spinl-7413,
  year={1997},
  doi={10.1016/S0006-3495(97)78283-3},
  title={Spin-label electron spin resonance studies on the interactions of lysine peptides with phospholipid membranes},
  number={5},
  volume={73},
  issn={0006-3495},
  journal={Biophysical Journal},
  pages={2546--2555},
  author={Kleinschmidt, Jörg and Marsh, Derek}
}

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    <dc:contributor>Kleinschmidt, Jörg</dc:contributor>
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    <dc:creator>Marsh, Derek</dc:creator>
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    <dcterms:title>Spin-label electron spin resonance studies on the interactions of lysine peptides with phospholipid membranes</dcterms:title>
    <dc:creator>Kleinschmidt, Jörg</dc:creator>
    <dcterms:issued>1997</dcterms:issued>
    <dcterms:abstract xml:lang="eng">The interactions of lysine oligopeptides with dimyristoyl phosphatidylglycerol (DMPG) bilayer membranes were studied using spin-labeled lipids and electron spin resonance spectroscopy. Tetralysine and pentalysine were chosen as models for the basic amino acid clusters found in a variety of cytoplasmic membrane-associating proteins, and polylysine was chosen as representative of highly basic peripherally bound proteins. A greater motional restriction of the lipid chains was found with increasing length of the peptide, while the saturation ratio of lipids per peptide was lower for the shorter peptides. In DMPG and dimyristoylphosphatidylserine host membranes, the perturbation of the lipid chain mobility by polylysine was greater for negatively charged spin-labeled lipids than for zwitterionic lipids, but for the shorter lysine peptides these differences were smaller. In mixed bilayers composed of DMPG and dimyristoylphosphatidylcholine, little difference was found in selectivity between spin-labeled phospholipid species on binding pentalysine. Surface binding of the basic lysine peptides strongly reduced the interfacial pK of spin-labeled fatty acid incorporated into the DMPG bilayers, to a greater extent for polylysine than for tetralysine or pentalysine at saturation. The results are consistent with a predominantly electrostatic interaction with the shorter lysine peptides, but with a closer surface association with the longer polylysine peptide.</dcterms:abstract>
    <dc:contributor>Marsh, Derek</dc:contributor>
    <dcterms:bibliographicCitation>First publ. in: Biophysical Journal 73 (1997), pp. 2546-2555</dcterms:bibliographicCitation>
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