Investigation of the interaction of myelin basic protein with phospholipid bilayers using solid-state NMR spectroscopy.
Interaction of bovine myelin basic protein and its constituent charge isomers (C1-C3) with phospholipid bilayers was studied using solid-state NMR experiments on model membranes. 31P NMR experiments on multilamellar vesicles and mechanically aligned bilayers were used to measure the degree of protein-induced disorder in the lipid headgroup region while 2H NMR data provided the disorder caused by the protein in the hydrophobic core of the bilayers. Our results suggest that MBP and its charge isomers neither fragment nor significantly disrupt DMPC, POPC, POPC:POPG, and POPE bilayers. These results demonstrate that the MBP-induced fragmentation of POPC bilayers is due to the freeze-thaw cycles used in the preparation of multilamellar vesicles and not due to intrinsic protein-lipid interactions.
Pointer-Keenan
Caroline D
CD
Department of Chemistry, University of Michigan, Ann Arbor, MI 48109-1055, USA.
Lee
Dong-Kuk
DK
Hallok
Kevin
K
Tan
Anmin
A
Zand
Robert
R
Ramamoorthy
Ayyalusamy
A
D008051:Lipid Bilayers / Q000737:chemistry*; D046911:Macromolecular Substances / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy; D008560:Membrane Fluidity; D021962:Membrane Microdomains / Q000737:chemistry*; D008565:Membrane Proteins / Q000737:chemistry*; D004676:Myelin Basic Protein / Q000737:chemistry*; D010743:Phospholipids / Q000737:chemistry*; D016062:Porosity; D011485:Protein Binding
D008051:Lipid Bilayers; D046911:Macromolecular Substances; D008565:Membrane Proteins; D004676:Myelin Basic Protein; D010743:Phospholipids