Related Experiment Video
Updated: May 2, 2026

An ELISA Based Binding and Competition Method to Rapidly Determine Ligand-receptor Interactions
Published on: March 14, 2016
Inhibition of ligand exchange kinetics via active-site trapping with an antibody fragment
David Oyen1, Jan Steyaert, John N Barlow
1Structural Biology Brussels, Vrije Universiteit Brussel , Pleinlaan 2, 1050 Brussels, Belgium.
Abstract:
We describe the first example of an inhibitory antibody fragment (nanobody ca1697) that binds simultaneously to an enzyme (the enzyme dihydrofolate reductase from Escherichia coli) and its bound substrate (folate). Binding of the antibody to the substrate causes a 20-fold reduction in the rate of folate exchange kinetics. This work opens up the prospect of designing new types of antibody-based inhibitors of enzymes and receptors through suitable design of immunogens.
More Related Videos
12:38Titration ELISA as a Method to Determine the Dissociation Constant of Receptor Ligand Interaction
Published on: February 15, 2018
14:43Microfluidic On-chip Capture-cycloaddition Reaction to Reversibly Immobilize Small Molecules or Multi-component Structures for Biosensor Applications
Published on: September 23, 2013
Related Concept Videos
Enzyme Inhibition
Ligand Binding Sites
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...
GPCR Desensitization
Enzymes
Enzyme deficiencies can often translate into life-threatening diseases. For example, a genetic abnormality resulting in the deficiency of the enzyme G6PD...
Immunoprecipitation
Chromatin Immunoprecipitation
Chromatin immunoprecipitation, also known as ChIP, is used to study protein-DNA or...
Antibody Actions
Neutralization
Antibodies can bind to pathogens, preventing them from infecting host cells. This process...