Quantitative Analysis of Receptor-Ligand Interactions at Equilibrium

Radioligand saturation binding for quantitative analysis of ligand-receptor interactions

The reversible combination of a ligand with specific sites on the surface of a receptor is one of the most important processes in biochemistry. A classic equation with a useful simple graphical method was introduced to obtain the equilibrium constant, Kd, and the maximum density of receptors, Bmax. The entire 125I-labeled ligand binding experiment includes three parts: the radiolabeling, cell s...

Analysis of Receptor-Ligand Interactions.

Structural Analysis of Chemokine Receptor–Ligand Interactions

This review focuses on the construction and application of structural chemokine receptor models for the elucidation of molecular determinants of chemokine receptor modulation and the structure-based discovery and design of chemokine receptor ligands. A comparative analysis of ligand binding pockets in chemokine receptors is presented, including a detailed description of the CXCR4, CCR2, CCR5, C...

Kinetic analysis of estrogen receptor/ligand interactions.

Surface plasmon resonance biosensor technology was used to directly measure the binding interactions of small molecules to the ligand-binding domain of human estrogen receptor. In a screening mode, specific ligands of the receptor were easily discerned from nonligands. In a high-resolution mode, the association and dissociation phase binding responses were shown to be reproducible and could be ...

Protein-blot analysis of receptor-ligand interactions.

Protein blotting was originally introduced as a solid-phase immunoassay (Gershoni & Palade, 1983; Towbin & Gordon, 1984). However, this technique can also be employed for the analysis of ligand-receptor interactions. In principle, a protein sample containing a receptor is resolved by gel electrophoresis and then blotted to an immobilizing matrix, such as a nitrocellulose membrane filter, as wou...