Related Experiment Video
Updated: Apr 28, 2026
12:18
Assembly of Cell Mimicking Supported and Suspended Lipid Bilayer Models for the Study of Molecular Interactions
Published on: August 3, 2021
3.2K
Albumin-fatty acid interactions at monolayer interface.
1Department of Biological Sciences, Faculty of Science and Technology, Sunway University, No. 5, Jalan Universiti, Bandar Sunway, Petaling Jaya, Selangor 46150, Malaysia ; Department of Chemistry, Faculty of Science, University of Malaya, Kuala Lumpur 50603, Malaysia.
Nanoscale Research Letters
|June 10, 2014
Summary
Researchers studied stearic acid (SA) and bovine serum albumin (BSA) interactions to mimic cell membranes. They found a specific mixture (0.8 BSA mole fraction) demonstrated maximum stability and strong lipid-protein attraction.
Area of Science:
- Biophysics
- Materials Science
Background:
- The fluid mosaic model describes protein embedding in cell membranes.
- Understanding lipid-protein interactions is crucial for membrane function.
Purpose of the Study:
- To investigate the interactions between stearic acid (SA) and bovine serum albumin (BSA) as model lipid-protein components.
- To mimic and analyze the normal membrane bilayer environment.
Main Methods:
- Utilized the Langmuir-Blodgett technique to create mixed SA-BSA monolayers on water.
- Recorded surface pressure (π)-molecular area (A) isotherms.
- Transferred mixed monolayers onto silicon wafers for atomic force microscopy (AFM) imaging.
- Analyzed miscibility, compressibility, and thermodynamic stability.
Main Results:
- A stable mixed system was identified at a BSA mole fraction (X BSA) of 0.8, showing large negative deviation of A ex and minimum ΔG ex.
- Compressibility analysis indicated a liquid-expanded phase below 50 mN m(-1) with strong SA-BSA interactions.
- AFM imaging confirmed strong attraction of BSA to the membrane surface, supporting quantitative data.
Conclusions:
- The SA-BSA mixture at X BSA = 0.8 represents the most thermodynamically stable configuration.
- Strong interactions occur between stearic acid and bovine serum albumin in the liquid-expanded phase.
- Experimental findings support the model of proteins being strongly attracted to lipid membrane surfaces.
Related Concept Videos
01:20Factors Affecting Protein-Drug Binding: Protein-Related Factors
701
Drug binding to proteins is a key aspect of pharmacokinetics and can influence a drug's distribution, absorption, and elimination in the body. Several factors, including the drug's physiochemical properties, protein concentration, disease states, and the number of binding sites on the protein, influence this process.
The physicochemical properties of a drug play a significant role in its ability to bind to proteins. Lipophilic drugs, which dissolve in fats, oils, and lipids, can be...
The physicochemical properties of a drug play a significant role in its ability to bind to proteins. Lipophilic drugs, which dissolve in fats, oils, and lipids, can be...
701
01:29Drug Distribution: Plasma Protein Binding
12.5K
Drugs predominantly attach to plasma proteins, with only a small percentage remaining unbound. The unbound portion can be calculated as one minus the bound fraction. Acidic drugs form large, inactive complexes by reversibly binding to plasma albumin, which prevents them from diffusing across biological barriers. These drug-protein complexes act as reservoirs for the drugs. As the concentration of unbound drugs decreases, these complexes quickly dissociate to release the free drug, maintaining...
12.5K
01:23Factors Affecting Protein-Drug Binding: Drug Interactions
726
Drug interactions are a critical aspect of pharmacology and can occur when two or more drugs compete for the same binding site. This competition can result in one drug displacing another, altering the effect of the displaced drug. Drug interactions are complex processes that rely heavily on how much of the displacer drug is present and how strongly it can bind to the same sites as the displaced drug.
Displacement interactions can have varying outcomes, ranging from toxicity to virtually...
Displacement interactions can have varying outcomes, ranging from toxicity to virtually...
726
01:35Asymmetric Lipid Bilayer
8.0K
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%...
8.0K
01:32Lipids as Anchors
6.0K
In the plasma membrane, the lipids forming the bilayer can also act as an anchor to tether proteins to the membrane. The three main types of lipid anchors found in eukaryotes are – prenyl groups, fatty acyl groups, and glycosylphosphatidylinositol or GPI groups. Prenyl and fatty acyl groups act as anchors on the cytosolic surface of the membrane, whereas GPI anchors proteins on the extracellular side.
The carboxy-terminal of most of the prenylated proteins, such as Ras proteins, contains...
The carboxy-terminal of most of the prenylated proteins, such as Ras proteins, contains...
6.0K
02:04Protein-protein Interfaces
12.5K
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
12.5K