Calypso Biomacromolecule Interaction Analyzer

Calypso Biomacromolecule Interaction AnalyzerIt is a bio macromolecule interaction analysis system based on component gradient multi angle light scattering (CG-MALLS), which can quickly, automatically, non destructively, and quantitatively characterize the interactions between macromolecules. It has many advantages such as high repeatability, high sensitivity, and no need for sample modification. This system can analyze the specific and non-specific interactions between molecules, as well as the dynamics of aggregation or dissociation. For specific intermolecular interactions, Calypso can determine their self aggregation and hetero aggregation between different sample molecules, obtaining the equilibrium dissociation constant Kd and the stoichiometric number of the reaction. For non-specific interactions, their dimensional coefficients can be determined, and the intermolecular forces and strengths can be determined. In addition, Calypso can also measure important molecular information such as reaction kinetics, sample weight average molecular weight, and root mean square radius.

The Calypso analysis system does not require modification of the sample (fluorescent labeling, immobilization, etc.), and is measured in a solution environment, thus ensuring the natural state of the sample to a large extent and obtaining results that are difficult to obtain by other technologies. It truly characterizes the interactions between biomolecules and facilitates sample recovery.

The working principle of the Calypso analysis system: Component Gradient Multi angle Light Scattering (CG-MALS) is one of the new analysis techniques that uses changes in molecular weight to determine intermolecular interactions. The scattering intensity of large molecules in a solution depends on the concentration C and weight average molecular weight Mw of the substance. Molecular recombination occurs, and Mw increases. For example, if all protein molecules appear in dimer form, the scattered light intensity will also increase by a factor of two. For reversible aggregation, the ratio of protein to monomeric protein complexes will reach an equilibrium value, which depends on the initial concentration of each protein and the conditions of the buffer solution. Different compositions and concentrations can lead to different Mw values. By analyzing a series of light scattering results with different compositions and concentrations, the aggregation forms that occur, their respective binding affinities Ka, and the equilibrium constants of binding and dissociation can be determined. Manual proportioning and measurement is a tedious, time-consuming, and prone to operational errors. The Calypso system overcomes the difficulties of CG-MALS manual operation through an automated process, integrating sample preparation, transportation, data collection, and analysis into one, perfectly ensuring the repeatability of experiments and solving the problem of introducing operational errors when manually preparing samples.

technical advantage
1. Intelligent sample preparation eliminates the error problem during manual sample preparation;
2. The sample is directly tested without the need for labeling or immobilization, ensuring the natural state of the sample to a large extent;
3. Quick measurement time, the experimental results can be obtained in half an hour;
4. Suitable for the determination of various biological reaction systems;
5. Analysis of self aggregation in the system and heteropolymerization of different sample molecules;
6. Analysis of stoichiometric point and equilibrium constant, equilibrium constant range: pM – mM;
7. Analysis of reaction kinetics;
8. Used in conjunction with laser detectors and concentration detectors to quickly determine the Mw, Rg, A2, A3 of substances; Obtain Zimm diagram;

Calypso Biomacromolecule Interaction AnalyzerApplication fields:
1. Enzyme reaction system: interaction between enzymes and inhibitors, enzymatic kinetics, etc
2. Drug exploration: the impact of drugs on protein-protein interactions, etc
3. Immunological research: interactions between antigens/antibodies, etc
4. Method improvement: Determine and adjust the second dimensional force coefficient to assist in purifying antibodies, determining the composition of polymers, and determining optimal dissolution conditions for samples.
5. Combining specificity: chemical stoichiometry point, equilibrium constant, ion strength, pH, or the influence of excipients on the binding of polymers or proteins.
6. Structural analysis of multi molecular complexes: Characterize the binding strength between molecules during the aggregation process of macromolecules under a series of buffer solutions, time, and temperature changes, and determine their stoichiometric relationships. Determine their spatial configuration through Mw and Rg.