Spin-label ESR studies on the interaction of bovine spinal cord myelin basic protein with dimyristoylphosphatidylglycerol dispersions.

Biochemistry
M B SankaramD Marsh

Abstract

Electron spin resonance (ESR) spectroscopy and chemical binding assays were used to study the interaction of bovine spinal cord myelin basic protein (MBP) with dimyristoylphosphatidylglycerol (DMPG) membranes. Increasing binding of MBP to DMPG bilayers resulted in an increasing motional restriction of PG spin-labeled at the C-5 atom position in the acyl chain, up to a maximum degree of association of 1 MBP molecule per 36 lipid molecules. ESR spectra of PG spin-labels labeled at other positions in the sn-2 chain showed a similar motional restriction, while still preserving the chain flexibility gradient characteristic of fluid lipid bilayers. In addition, labels at the C-12 and C-14 atom positions gave two-component spectra, suggesting a partial hydrophobic penetration of the MBP into the bilayer. Spectral subtractions were used to quantitate the membrane penetration in terms of the stoichiometry of the lipid-protein complexes. Approximately 50% of the spin-labeled lipid chains were directly affected at saturation protein binding. The salt and pH dependence of the ESR spectra and of the protein binding demonstrated that electrostatic interaction of the basic residues of the MBP with the PG headgroups is necessary for an effecti...Continue Reading

Citations

Jan 1, 1991·The International Journal of Biochemistry·T Cserháti, M Szögyi
Mar 17, 2010·The Journal of Physical Chemistry. B·Candace M Pfefferkorn, Jennifer C Lee
Aug 1, 1990·FEBS Letters·D Marsh
Aug 2, 2008·Methods : a Companion to Methods in Enzymology·Derek Marsh
Nov 3, 2004·Biochimica Et Biophysica Acta·Derek Marsh, Tibor Páli
Oct 2, 2007·Biophysical Journal·Carla M Rosetti, Bruno Maggio
Feb 26, 2008·Biochimica Et Biophysica Acta·Derek Marsh
Mar 19, 1991·Biochemistry·P MeersD Papahadjopoulos
Nov 1, 1992·Journal of Neurochemistry·R Smith

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