Wyatt Technology launches its new Calypso automated protein association and aggregation system

Wyatt Technology Inc. has launched its new Calypso™ automated protein association and aggregation system. This instrument package enables the rapid, quantitative, nondestructive characterization of protein-protein interactions in native solution using composition-gradient multi-angle light scattering (CG-MALS).

Interactions between proteins are at the heart of many biological functions and are of great importance for every process in a living cell. Information about how proteins such as enzymes and inhibitors interact, improves our understanding of diseases and can point to new therapeutic approaches. Characterization of protein aggregation is critical to the pharmaceutical and biotechnology industries, where it is particularly important that the protein is in the solution phase in specific formulation buffers. There are numerous methods for detecting protein interactions and aggregation kinetics, each varying in sensitivity and specificity. CG-MALS is an ideal means for measuring the proteins in their native solution:, protein samples need not be tagged, immobilized on a surface, or otherwise modified from their natural state. It is a sensitive and precise method for the measurement of complexes and aggregates through the absolute determination of molar mass and can non-destructively characterize both weak and strong interactions. Simple or complex association stoichiometries may be analyzed, providing equilibrium dissociation constants from picomolars to millimolars, as well as self- and cross- viral coefficients and aggregation or association kinetics.

The Wyatt Calypso system consists of hardware and dedicated software for automating CG-MALS measurements as well as Zimm plots and dn/dc determinations. Computer-controlled syringe pumps automate the sample mixing, dilution and delivery, while intuitive software controls the experiment, acquires data and analyzes the results. The system can also be used to facilitate the study of the composition dependence of any measurable solution property (spectroscopic, hydrodynamic, calorimetric).