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PMID: 7407163 Published · ppublish English Journal Article

The influence of poly(L-lysine) on phospholipid polymorphism. Evidence that electrostatic polypeptide-phospholipid interactions can modulate bilayer/non-bilayer transitions.

Biochimica et biophysica acta ·Vol. 601 ·No. 1 ·1980-09-02 ·Pages 235-40

de Kruijff B, Cullis PR

Abstract

31P-NMR shows that poly(L-lysine) binding to cardiolipin, phosphatidylserine or phosphatidylglycerol does not affect the macroscopic structure or local order (in the phosphate region) of the phospholipids. In the case of cardiolipin poly(L-lysine) inhibits the ability of Ca2+ to induce the hexagonal HII phase. Alternatively, poly(L-lysine) induces the hexagonal HII phase for a fraction of the phospholipids in phosphatidylethanolamine-cardiolipin (2:1) dispersions.

MeSH Terms
Calcium Cardiolipins Lipid Bilayers Liposomes Magnetic Resonance Spectroscopy Molecular Conformation Peptides Phosphatidylglycerols Phosphatidylserines Phospholipids Polylysine Protein Binding
Chemicals
Cardiolipins Lipid Bilayers Liposomes Peptides Phosphatidylglycerols Phosphatidylserines Phospholipids Polylysine Calcium
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
de Kruijff B
Cullis P R
Article Info
Journal
Biochimica et biophysica acta
Abbr.
Biochim Biophys Acta
ISSN
0006-3002
Published
1980-09-02
Pages
235-40
Language
English
Region
Netherlands
NLM ID
0217513
Subset
IM
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