Calypso II
Rapid, automated, quantitative characterization of macromolecular interactions
Composition-Gradient Multi-Angle Light Scattering (CG-MALS) employs a series of unfractionated samples of different composition or concentration in order to characterize macromolecular interactions such as reversible self- and hetero-association of proteins, reaction rates and affinities of irreversible aggregation, or virial coefficients. No special modifications - e.g. sample tagging or immobilization procedures - are necessary: samples are entirely in solution.
The primary analysis techniques supported by Calypso are:
- Strong, specific reversible interactions: Kd (equilibrium dissociation constant) from picomolars to millimolars; stoichiometries of associating complexes; self and/or heteroassociations.
- Weak, non-specific interactions: self- and cross-virial coefficients
- Aggregation and other time-dependent reactions: stop-flow kinetics; t (equilibration or relaxation time) from seconds to hours.
- Zimm plots: concentration gradients for determining MW (weight-averaged molar mass); A2, A3 (second and third virial coefficients); rg (root mean square radius, a.k.a. "radius of gyration")
- Refractive increment: dn/dc
Calypso's automation enhances productivity by improving repeatability and reliability, while minimizing time and effort. Compared to other techniques for characterizing protein interactions - as well as manual CG-MALS measurements - Calypso provides fast and accurate results.
Applications:
Drug Discovery:
- Quantify binding affinity and stoichiometry of enzyme/inhibitor or antibody/antigen interactions
- Study the impact of small molecules on protein-protein interactions.
Process Improvement:
- Determine second virial coefficient and adjust buffer parameters to improve formulation stability and viscosity
- Determine cross virial coefficients to optimize antibody purification and understand the effects of large excipients on formulations.
Self-assembly/Aggregation:
- Quantify impact of solvent ionic strength, pH, or excipients on polymerization or protein associations.
- Measure kinetics of self-assembly and aggregation via rate of change of molar mass and radius of gyration
Biotech R&D:
- Characterize macromolecular binding affinity and associated complex stoichiometry over a wide range of buffer compositions, time, and temperature scales.
Application Notes:
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Description
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Download
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| 13 |
Does Antithrombin III Block the Action of a Monoclonal
Anti-Thrombin Antibody?
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| 12 |
Measuring the Interaction Between Thrombin-α
and an Anti-Thrombin Antibody
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| 11 |
Determining the Kinetics of Covalent Thrombin-Antithrombin Association
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| 10 |
Binding Affinity and Stoichiometry of a Multivalent
Protein-aptamer Association
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| 09 |
Rapid, Autonomous Lot-to-Lot Comparability of
Monoclonal Antibodies with the Calypso
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| 08 |
Measuring Anti-body-Antigen Interactions with the Calypso
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| 07 |
Kinetics of Enzyme-Inhibitor Associations
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| 06 |
Characterization of Heparin Binding to Tau Protein via CG-MALS
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| 05 |
Standard Zimm Plot
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| 04 |
Reversible Self - Association
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| 03 |
Composition Gradient Static Light Scattering: A Powerful Tool for the Detection and Characterization of Reversible Macromolecular Associations
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| 02 |
Continuous Flow for Faster Determinations of Mw and A2
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| 01 |
Characterization of Reversible Hetero-Association with Calypso
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