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Interaction of Myelin Basic Protein with Myelin-like Lipid Monolayers at Air-Water Interface.

Langmuir : the ACS journal of surfaces and colloids (2018-05-04)
Katharina Widder, Jennica Träger, Andreas Kerth, George Harauz, Dariush Hinderberger
RESUMO

Interaction of myelin basic protein (MBP) and the cytoplasmic leaflets of the oligodendrocyte membrane is essential for the formation and compaction of the myelin sheath of the central nervous system and is altered aberrantly and implicated in the pathogenesis of neurodegenerative diseases like multiple sclerosis. To gain more detailed insights into this interaction, the adsorption of MBP to model lipid monolayers of similar composition to the myelin of the central nervous system was studied at the air-water interface with monolayer adsorption experiments. Measuring the surface pressure and the related maximum insertion pressure of MBP for different myelin-like lipid monolayers provided information about the specific role of each of the single lipids in the myelin. Depending on the ratio of negatively charged lipids to uncharged lipids and the distance between charges, the adsorption process was found to be determined by two counteracting effects: (i) protein incorporation, resulting in an increasing surface pressure and (ii) lipid condensation due to electrostatic interaction between the positively charged protein and negatively charged lipids, resulting in a decreasing surface pressure. Although electrostatic interactions led to high insertion pressures, the associated lipid condensation lowered the fluidity of the myelin-like monolayer.

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Avanti
Brain PS, Avanti Research - A Croda Brand
Avanti
Brain SM, Avanti Research - A Croda Brand
Avanti
Liver PI, Avanti Research - A Croda Brand
Sigma-Aldrich
NSC 632839, ≥98% (HPLC)
Avanti
Brain PE, Avanti Research - A Croda Brand 840022P, powder
Avanti
Brain PC, Avanti Research - A Croda Brand 840053P, powder