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Related Concept Videos

Asymmetric Lipid Bilayer01:35

Asymmetric Lipid Bilayer

Biological membranes show uneven distribution of different types of lipids in the inner and outer layers, resulting in transverse asymmetric membranes. The treatment of the erythrocyte membrane with the enzyme phospholipase confirmed the asymmetric nature of the lipid bilayer. The enzyme hydrolyzes lipids into fatty acids and hydrophilic groups. The phospholipase acts only on the outer layer of the membrane, while the inner layer remains intact. The phospholipase treatment resulted in 80%...
Mechanisms of Membrane-bending01:15

Mechanisms of Membrane-bending

The living membranes are flexible due to their fluid mosaic nature; however, their bending into different shapes is an active process regulated by specific lipids and proteins. The membrane bending can be transient as seen in vesicles or stable for a long time as in microvilli. Cells regulate the size, location, and duration of the membrane curvature.
Membrane bending can happen due to intrinsic changes in lipid composition or extrinsic association with different proteins. The proteins involved...
Membrane Fluidity01:26

Membrane Fluidity

Membrane fluidity is explained by the fluid mosaic model of the cell membrane, which describes the plasma membrane structure as a mosaic of components—including phospholipids, cholesterol, proteins, and carbohydrates—that gives the membrane a fluid character.
Mosaic nature of the membrane
The mosaic characteristic of the membrane helps the plasma membrane remain fluid. The integral proteins and lipids exist as separate but loosely-attached molecules in the membrane. The membrane is a relatively...
Membrane Fluidity01:23

Membrane Fluidity

Cell membranes are composed of phospholipids, proteins, and carbohydrates loosely attached to one another through chemical interactions. Molecules are generally able to move about in the plane of the membrane, giving the membrane its flexible nature called fluidity. Two other features of the membrane contribute to membrane fluidity: the chemical structure of the phospholipids and the presence of cholesterol in the membrane.Fatty acids tails of phospholipids can be either saturated or...
Membrane Asymmetry Regulating Transporters01:19

Membrane Asymmetry Regulating Transporters

Enzymes like flippase, floppase, and scramblase transfer phospholipids from one layer to another in the membrane, thereby affecting membrane asymmetry.
Flippase
Eukaryotic flippases are type-IV P-type ATPases or P4-ATPases belonging to P-type ATPase family proteins that are membrane-bound pumps involved in the ATP-mediated transport of ions and molecules across the membrane. Flippases flip specific phospholipids from the outer to the inner leaflet of a membrane. All P4-ATPases have one...
Membrane Domains01:18

Membrane Domains

The membrane domains concentrate specific lipids and proteins at one place within the membrane, which helps in cell signaling, adhesion, and other critical cellular processes. These domains can differ in size, composition, function, and lifespan.
Protein Domains
The membrane comprises a group of distinct proteins responsible for carrying out a cell's specific function. For example, the plasma membrane of the human sperm, or a single germ cell, contains a unique set of proteins in the anterior...

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Related Experiment Video

Updated: Jul 17, 2026

Preparation and Immunostaining of Myelinating Organotypic Cerebellar Slice Cultures
09:41

Preparation and Immunostaining of Myelinating Organotypic Cerebellar Slice Cultures

Published on: March 20, 2019

Myelin basic protein binding is modulated by leaflet asymmetry and lipid composition.

Julio M Pusterla1, Alexandros Koutsioubas2, Nicolò Paracini3

  • 1Jülich Centre for Neutron Science (JCNS-1), Forschungszentrum Jülich GmbH, Leo-Brandt Straße, 52428 Jülich, Germany.

Journal of Colloid and Interface Science
|July 15, 2026
PubMed
Summary

Lipid asymmetry in cell membranes is crucial for protein interactions. Myelin Basic Protein binds best to asymmetric myelin membranes, with altered binding in disease states.

Keywords:
Membrane asymmetryMyelinMyelin basic proteinNeutron reflectometrySelective deuterationSupported lipid bilayer

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Last Updated: Jul 17, 2026

Preparation and Immunostaining of Myelinating Organotypic Cerebellar Slice Cultures
09:41

Preparation and Immunostaining of Myelinating Organotypic Cerebellar Slice Cultures

Published on: March 20, 2019

Lipid-Protein Membrane Structure-Function Characterization using Droplet Interface Bilayers
10:27

Lipid-Protein Membrane Structure-Function Characterization using Droplet Interface Bilayers

Published on: June 12, 2026

Realistic Membrane Modeling Using Complex Lipid Mixtures in Simulation Studies
07:31

Realistic Membrane Modeling Using Complex Lipid Mixtures in Simulation Studies

Published on: September 1, 2023

Area of Science:

  • Biochemistry
  • Membrane Biophysics
  • Neuroscience

Background:

  • Cell membrane asymmetry is vital for biological functions.
  • Lipid composition influences protein interactions within membranes.
  • Myelin Basic Protein (MBP) plays a key role in myelin sheath stability.

Purpose of the Study:

  • To investigate the impact of leaflet-specific lipid composition on MBP binding to biomimetic myelin membranes.
  • To understand how myelin membrane asymmetry affects MBP interactions.
  • To explore changes in MBP binding in disease-mimicking compositions.

Main Methods:

  • Neutron reflectometry was employed to study biomimetic myelin bilayers.
  • Asymmetric supported myelin bilayers with deuterated cholesterol were constructed.
  • MBP binding was quantified under conditions of varying lipid asymmetry and composition.

Main Results:

  • MBP preferentially binds to asymmetric myelin bilayers mimicking native myelin.
  • Experimental Autoimmune Encephalomyelitis-modified compositions showed weaker MBP binding and increased protein insertion.
  • Disrupting lipid asymmetry significantly reduced MBP binding, irrespective of membrane charge.

Conclusions:

  • Lipid asymmetry is a critical determinant of MBP-membrane interactions.
  • Altered lipid composition and asymmetry impact MBP binding, relevant to demyelination.
  • Findings provide insights into myelin stability and the molecular basis of neurological disorders.