Wyatt Technology Corporation has announced the availability of an application note demonstrating the advanced capability of composition gradient multi-angle light scattering (CG-MALS) technology.
The experiment assessed the performance of the company's Calypso automated composition gradient light scattering system for the evaluation of the inhibition efficacy of AEBSF, a small-molecule irreversible inhibitor, on the self association of the a-chymotrypsin digestive enzyme.
The Calypso is able to accurately and rapidly analyse the inhibition kinetics of protein-protein binding as well as equilibrium association properties.
The application note, entitled 'Inhibition Kinetics of Protein-Protein Binding with Calypso', is available to download free of charge via Wyatt's website.
CG-MALS is a non-destructive method for efficiently characterising macromolecular interactions without labelling, immobilisation or additional biochemical substrates.
It employs a series of samples of different compositions or concentrations in order to characterise the reversible self- and hetero-association of proteins, reaction rates and affinities of aggregation or dissociation and non-specific, repulsive or attractive macromolecular interactions.
The Calypso offers analytical capabilities, simplifying and automating CG-MALS measurements.
The system's automation enhances productivity by improving repeatability and reliability, while minimising time and effort.
The Calypso offers many advantages over other biophysical techniques for characterising protein interactions, providing fast and accurate results.
The application note describes the CG-MALS method using the Calypso automated composition gradient system.
The instrument is used in conjunction with Wyatt Technology's Dawn-Heleos and Minidawn-Treos MALS detectors and an optional dRI or UV absorption online concentration detector.
Experimental results demonstrate that the dissociation rate is dependent on the concentrations of protein and inhibitor, determining both the protein-inhibitor kinetics parameter kM and protein homodimer dissociation constant Kd.
