Related Experiment Video
Updated: Aug 15, 2026

10:49
Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
Published on: March 5, 2017
Lipid membrane reorganization induced by chemical recognition
J A Last1, T A Waggoner, D Y Sasaki
1Biomolecular Materials and Interfaces Department, Sandia National Laboratories, Albuquerque, New Mexico 87185, USA.
Biophysical Journal
|October 19, 2001
Summary
Chemical recognition triggers nanoscale changes in lipid membranes. Copper ion binding alters lipid domains, and EDTA removes ions, reversing the effect, demonstrating dynamic membrane reorganization.
Area of Science:
- Biophysics
- Materials Science
- Nanotechnology
Background:
- Lipid bilayer membranes exhibit complex nanoscale structures.
- Chemical recognition events can influence membrane organization.
- Atomic Force Microscopy (AFM) allows high-resolution imaging of membrane surfaces.
Purpose of the Study:
- To image nanoscale structural reorganization in lipid bilayers induced by chemical recognition.
- To investigate the effect of copper ion (Cu2+) binding on lipid membrane domains.
- To demonstrate the reversibility of chemically induced membrane structural changes.
Main Methods:
- In situ Atomic Force Microscopy (AFM) for high-resolution imaging.
- Utilizing supported lipid bilayers composed of distearoylphosphatidylcholine (DSPC) and a synthetic Cu2+ receptor-functionalized lipid.
- Inducing changes via Cu2+ binding and reversing them using EDTA.
Main Results:
- Phase separation into nanoscale domains with a 9 A height difference was observed.
- Cu2+ binding altered the receptor's electrostatic nature, leading to dispersion.
- Receptor dispersion caused shrinking of membrane structural features defined by receptors.
- EDTA successfully removed metal ions, demonstrating complete process reversibility.
Conclusions:
- Chemical recognition events can induce dynamic nanoscale structural reorganization in lipid membranes.
- The study visualizes the reversible dispersion of functionalized lipids upon metal ion binding.
- AFM is a powerful tool for observing real-time, chemically induced changes in lipid bilayer nanostructures.
Related Concept Videos
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 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...
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...
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%...
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...
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...
Assembly of the Lipid Bilayer in the ER
Biological membranes are more than just a barrier separating cell cytoplasm from the outside environment. They are highly dynamic and help maintain the integrity and physiological stability of the cells as well as membrane-bound organelles. Membranes also play vital roles in cell-to-cell and intracellular communication.
A large chunk of any biological membrane is composed of phospholipids. These lipids have a heterogeneous distribution across different subcellular organelles and even between...
A large chunk of any biological membrane is composed of phospholipids. These lipids have a heterogeneous distribution across different subcellular organelles and even between...
Mechanisms of Membrane Domain Formation
Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
Another mechanism for membrane domain formation involves membrane proteins interacting with cytoskeletal...
Another mechanism for membrane domain formation involves membrane proteins interacting with cytoskeletal...

