scholarly journals Different Head Group Dependence on The Lipid Thermodynamic Property of Myelin Basic Protein in the Lipid Monolayer

2021 ◽  
Author(s):  
Lei Zhang ◽  
Ming Zhang ◽  
Runguang Sun
Keyword(s):  
Myelin Basic Protein ◽  
Electrostatic Interactions ◽  
Basic Protein ◽  
Second Virial Coefficient ◽  
Virial Equation ◽  
Lipid Monolayer ◽  
Statistical Thermodynamic ◽  
Head Group ◽  
Myelin Lipid ◽  
Head Groups

Abstract The interaction between the role of 18.5 KDa myelin basic protein (MBP) isoform and phospholipids has been thought to maintain the stability and compactness of the myelin sheath structure. In this study, we describe the statistical thermodynamic theory of different concentrations’ effects on MBP in the major myelin lipid (1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC), 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine (POPE)，and 1-palmitoyl-2-oleoyl-sn-glycero-3-phospho-L-serine (POPS)) monolayers at the air/subphase interface via Langmuir-Blodgett (LB) technique. A simple statistical mechanical theory is established that predicts the interaction between proteins and phosphate head groups at low surface pressures and the second virial coefficient dependences for the PC, PE, and PS head groups are illustrated. In addition, the surface pressure(π)-mean molecular area(mma) curves were also analyzed using two-dimensional virial equation of state (2D-VES). The positively charged showed that MBP may integrate into different lipid monolayers via hydrophobic and electrostatic interactions, which was found to be consistent with AFM observations of domain and aggregate structures as well as with changes in the surface morphology induced by MBP. These analyses pertaining to membrane structure will provide better insight into membrane modeling systems, especially the interaction between membrane molecules.

scholarly journals Interaction forces and adhesion of supported myelin lipid bilayers modulated by myelin basic protein

2009 ◽  
Vol 106 (9) ◽  
pp. 3154-3159 ◽  
Author(s):  
Y. Min ◽  
K. Kristiansen ◽  
J. M. Boggs ◽  
C. Husted ◽  
J. A. Zasadzinski ◽  
...  
Keyword(s):  
Myelin Basic Protein ◽  
Lipid Bilayers ◽  
Basic Protein ◽  
Myelin Lipid ◽  
Interaction Forces

scholarly journals Polyunsaturated fatty acids produce a range of activators for heterogeneous IKs channel dysfunction

2019 ◽  
Vol 152 (2) ◽  
Author(s):  
Briana M. Bohannon ◽  
Xiaoan Wu ◽  
Xiongyu Wu ◽  
Marta E. Perez ◽  
Sara I. Liin ◽  
...  
Keyword(s):  
Ventricular Arrhythmias ◽  
Electrostatic Interactions ◽  
Voltage Dependence ◽  
Delayed Rectifier ◽  
Head Group ◽  
Maximal Conductance ◽  
Head Groups ◽  
K Current ◽  
Iks Channel ◽  
Congenital Long Qt Syndrome

Repolarization and termination of the ventricular cardiac action potential is highly dependent on the activation of the slow delayed-rectifier potassium IKs channel. Disruption of the IKs current leads to the most common form of congenital long QT syndrome (LQTS), a disease that predisposes patients to ventricular arrhythmias and sudden cardiac death. We previously demonstrated that polyunsaturated fatty acid (PUFA) analogues increase outward K+ current in wild type and LQTS-causing mutant IKs channels. Our group has also demonstrated the necessity of a negatively charged PUFA head group for potent activation of the IKs channel through electrostatic interactions with the voltage-sensing and pore domains. Here, we test whether the efficacy of the PUFAs can be tuned by the presence of different functional groups in the PUFA head, thereby altering the electrostatic interactions of the PUFA head group with the voltage sensor or the pore. We show that PUFA analogues with taurine and cysteic head groups produced the most potent activation of IKs channels, largely by shifting the voltage dependence of activation. In comparison, the effect on voltage dependence of PUFA analogues with glycine and aspartate head groups was half that of the taurine and cysteic head groups, whereas the effect on maximal conductance was similar. Increasing the number of potentially negatively charged moieties did not enhance the effects of the PUFA on the IKs channel. Our results show that one can tune the efficacy of PUFAs on IKs channels by altering the pKa of the PUFA head group. Different PUFAs with different efficacy on IKs channels could be developed into more personalized treatments for LQTS patients with a varying degree of IKs channel dysfunction.

scholarly journals Effect of Cholesterol and Myelin Basic Protein (MBP) Content on Lipid Monolayers Mimicking the Cytoplasmic Membrane of Myelin

Cells ◽  
2020 ◽  
Vol 9 (3) ◽  
pp. 529 ◽  
Author(s):  
Jennica Träger ◽  
Katharina Widder ◽  
Andreas Kerth ◽  
George Harauz ◽  
Dariush Hinderberger
Keyword(s):  
Myelin Basic Protein ◽  
Lipid Membranes ◽  
Cytoplasmic Membrane ◽  
Basic Protein ◽  
Cholesterol Content ◽  
Demyelinating Diseases ◽  
Lipid Monolayer ◽  
Lipid Monolayers ◽  
Additional Imaging ◽  
The Central Nervous System

Myelin basic protein (MBP) is located in the insulating covers of nerve cells in the brain and spinal cord. By interacting with lipid membranes, it is responsible for compaction of the myelin sheath in the central nervous system, which is weakened in demyelinating diseases. The lipid composition of the myelin leaflet has a high impact on the interaction between the membrane and MBP. Cholesterol is present in the cytoplasmic leaflet with a rather high amount of 44% (mol%). In this study, the focus is on the effect of cholesterol, mainly by varying its content, on the interaction of MBP with a lipid monolayer. Therefore, Langmuir lipid monolayers mimicking the cytoplasmic membrane of myelin and monolayers with variations of cholesterol content between 0% and 100% were measured at the air/water interface with additional imaging by fluorescence microscopy. All experiments were performed with and without bovine MBP to study the dependence of the interaction of the protein with the monolayers on the cholesterol content. The native amount of 44% cholesterol in the monolayer combines optima in the order of the monolayer (presumably correlating to compaction and thermodynamic stability) and protein interaction and shows unique features in comparison to lower or higher cholesterol contents.

Electron Microscopy of Myelin Basic Protein (MBP) Organized as Planar Arrays on a Lipid Monolayer Surface: Deimination of MBP Hinders Its Organizational Properties

2000 ◽  
Vol 6 (S2) ◽  
pp. 250-251
Author(s):  
N. Ishiyama ◽  
P. Matharu ◽  
I.R. Bates ◽  
D.D. Wood ◽  
M.A. Moscarello ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Myelin Basic Protein ◽  
Basic Protein ◽  
Close Association ◽  
Iminodiacetic Acid ◽  
Lipid Monolayer ◽  
Nickel Salt ◽  
Acute Case ◽  
Planar Arrays ◽  
The Central Nervous System

Myelin basic protein (MBP) is one of the principal constituents of the mammalian myelin sheath. It is a basic peripheral membrane protein in the major dense line and is believed to play a structural role in maintaining myelin stability through its close association with lipids and other proteins. Immune responses to MBP have been implicated in the pathogenesis of multiple sclerosis (MS), the most common autoimmune disease of the central nervous system in North America and Northern Europe. The correlation between the severity of MS and the deimination of arginyl to citrullinyl residues in MBP was well illustrated in the acute case of MS (Marburg type) that contained MBP with 18 out of 19 arginines citrullinated.We have studied a recombinant hexahistidine-tagged murine MBP (rmMBP, 18.5 kDa isoform) by electron microscopy of the protein organized as planar arrays on lipid monolayers that consisted of the nickel chelating lipid, l,2-dioleoyl-.yn-glycero-3-[(N(5-amino-l-carboxypentyl)iminodiacetic acid)succinyl] (Nickel salt) (Ni2+-NTADOGS), and the filler lipid, liver phosphatidylinositol (PI).

scholarly journals Phase Transition Behaviors And Interactions And Adhesion Of Myelin Lipid Membranes Modulated By Myelin Basic Protein

2009 ◽  
Vol 96 (3) ◽  
pp. 611a-612a
Author(s):  
Younjin Min ◽  
Kai Kristiansen ◽  
Joan M. Boggs ◽  
Cynthia Husted ◽  
Joseph A. Zasadzinski ◽  
...  
Keyword(s):  
Phase Transition ◽  
Myelin Basic Protein ◽  
Lipid Membranes ◽  
Basic Protein ◽  
Myelin Lipid

scholarly journals Interaction of glycosphingolipids with melittin and myelin basis protein in monolayers

1981 ◽  
Vol 193 (2) ◽  
pp. 643-646 ◽  
Author(s):  
G D Fidelio ◽  
B Maggio ◽  
F A Cumar ◽  
R Caputto
Keyword(s):  
Myelin Basic Protein ◽  
Surface Pressure ◽  
Protein Interaction ◽  
Protein Concentration ◽  
Basic Protein ◽  
Head Group ◽  
Polar Head Group ◽  
Initial Surface ◽  
Lipid Protein Interaction ◽  
Modification Of The Surface

The penetration of melittin and myelin basic protein into glycosphingolipid monolayers depends on the lipid polar head group, the protein concentration available and the initial surface pressure. The lipid-protein interaction leads to modification of the surface properties of both the glycosphingolipid and the proteins.

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