Related Experiment Video
Updated: Feb 1, 2026
09:25
Lectin-based Isolation and Culture of Mouse Embryonic Motoneurons
Published on: September 15, 2011
18.6K
Evaluation of hetero-multivalent lectin binding using a turbidity-based emulsion agglutination assay
Nolan C Worstell1, Akshi Singla1, Hung-Jen Wu1
1Dept. of Chemical Engineering, Texas A&M University, College Station, TX, 77843, USA.
Colloids and Surfaces. B, Biointerfaces
|December 7, 2018
Summary
A new turbidity-based emulsion agglutination (TEA) assay enables high-throughput screening of molecular libraries for lectin hetero-multivalent binding. This method quantifies binding strength using emulsions, offering a customizable tool for ligand discovery.
Area of Science:
- Biochemistry
- Microbiology
- Molecular Biology
Background:
- Lectin hetero-multivalency, involving binding to multiple ligand types, is crucial for pathogens like *Pseudomonas aeruginosa* (LecA) and *Vibrio cholerae* (Cholera Toxin subunit B).
- Identifying ligands involved in this complex binding is essential for understanding pathogen mechanisms and developing therapeutics.
Purpose of the Study:
- To develop a high-throughput screening assay for identifying ligand candidates involved in lectin hetero-multivalent binding.
- To establish a method that minimizes common bottlenecks in ligand screening, such as surface functionalization.
Main Methods:
- A turbidity-based emulsion agglutination (TEA) assay was developed for high-throughput screening.
- Emulsions were formed using ultrasonication, and changes in turbidity were measured to quantify lectin-induced aggregation rates.
- The assay determines relative binding strengths between different ligand combinations.
Main Results:
- The TEA assay successfully quantified lectin-induced aggregation rates, reflecting relative binding strengths.
- Results obtained from the TEA assay were consistent with previous findings using a nanocube sensor.
- The assay demonstrated its capability for high-throughput screening of potential hetero-multivalent binding ligands.
Conclusions:
- The developed TEA assay is a robust, high-throughput, and customizable tool for screening ligands involved in hetero-multivalent binding.
- This assay simplifies the screening process by utilizing emulsions and minimizing substrate functionalization.
- TEA provides a valuable method for advancing research in molecular interactions and pathogen adhesins.
Related Concept Videos
02:45Blood Transfusion and Agglutination
14.7K
Blood transfusion is a therapeutic measure to restore the blood volume after extensive blood loss due to an accident or a medical procedure. Blood transfusion involves drawing a certain amount of blood from a suitable donor and infusing it into the recipient.
History
The history of blood transfusion dates back to the 17th century, when early attempts were made in animals. In 1818 James Blundell, a British doctor, performed the first successful human blood transfusion. Later in 1900, Karl...
History
The history of blood transfusion dates back to the 17th century, when early attempts were made in animals. In 1818 James Blundell, a British doctor, performed the first successful human blood transfusion. Later in 1900, Karl...
14.7K
02:18The Equilibrium Binding Constant and Binding Strength
15.0K
The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium:
15.0K
02:18The Equilibrium Binding Constant and Binding Strength
10.0K
10.0K
02:13Nuclear Binding Energy
14.8K
The difference between the calculated and experimentally measured masses is known as the mass defect of the atom. In the case of helium-4, the mass defect indicates a “loss” in mass of 4.0331 amu – 4.0026 amu = 0.0305 amu. The loss in mass accompanying the formation of an atom from protons, neutrons, and electrons is due to the conversion of that mass into energy that is evolved as the atom forms. The nuclear binding energy is the energy produced when the atoms’ nucleons are bound...
14.8K
02:40Ligand Binding Sites
15.1K
Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
15.1K
01:49Conserved Binding Sites
5.2K
Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
5.2K