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

被引:18
|
作者
Widder, Katharina [1 ]
Traeger, Jennica [1 ]
Kerth, Andreas [1 ]
Harauz, George [2 ]
Hinderberger, Dariush [1 ]
机构
[1] Martin Luther Univ Halle Wittenberg, Inst Chem, Von Danckelmann Pl 4, D-06120 Halle, Saale, Germany
[2] Univ Guelph, Dept Mol & Cellular Biol, 50 Stone Rd East, Guelph, ON N1G 2W1, Canada
基金
加拿大自然科学与工程研究理事会;
关键词
MULTIPLE-SCLEROSIS; POSTTRANSLATIONAL MODIFICATIONS; MEMBRANE INTERACTIONS; CONDENSED COMPLEXES; BINDING; PEPTIDES; 18.5-KDA; CHOLESTEROL; DOMAINS; CHARGE;
D O I
10.1021/acs.langmuir.8b00321
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
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.
引用
收藏
页码:6095 / 6108
页数:14
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