Interaction of the pore-forming domain of colicin A with phospholipid vesicles
- 19 September 1989
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 28 (19) , 7713-7719
- https://doi.org/10.1021/bi00445a029
Abstract
The interaction of the 20-kDa pore-forming domain of colcin A with phospholipid vesicles was investigated by gel permeation chromatography, analytical centrifugation, and electron microscopy. Under the experimental conditions of this study, this peptide was found to interact only with vesicles containing negatively charged phospholipids. It forms a well-defined dislike complex with phosphatidyglycerols with a preference for those containing 12-14 atoms of carbon in their fatty acid chain. This complex has a diameter of 120 .ANG. and is about one bilayer thick. It contains nine molecules of peptide and is formed both at acidic pH (pH 5.0) and at neutral pH (pH 7.2).This publication has 15 references indexed in Scilit:
- Interaction of colicin A with phospholipid monolayers and liposomesBiochemistry, 1983
- Amphipathic helix and its relationship to the interaction of calcitonin with phospholipidsBiochemistry, 1983
- Isolation, molecular and functional properties of the C-terminal domain of colicin A.The EMBO Journal, 1983
- The spontaneous insertion of proteins into and across membranes: The helical hairpin hypothesisCell, 1981
- Effect of colicins Ia and E1 on ion permeability of liposomes.Proceedings of the National Academy of Sciences, 1979
- Colicin K acts by forming voltage-dependent channels in phospholipid bilayer membranesNature, 1978
- Amphipathic helixes and plasma lipoproteins: Thermodynamic and geometric considerationsChemistry and Physics of Lipids, 1977
- Determination of molecular weight of the protein moiety in protein-detergent complexes without direct knowledge of detergent binding.Proceedings of the National Academy of Sciences, 1976
- Regulation of glutamine synthetase. XII. Electron microscopy of the enzyme from Escherichia coliBiochemistry, 1968
- Equilibrium Ultracentrifugation of Dilute Solutions*Biochemistry, 1964