Label-free and immobilization-free, CG-MALS is a rigorous yet versatile first-principles technique that measures interactions directly by monitoring the changes in solution molar mass that arise from the formation or dissociation of complexes. Apply CG-MALS to characterize:
- Self- and hetero-association
- Binding affinity from pM to mM
- Absolute molecular stoichiometry (not just mole ratios)
- Multi-valent or cooperative interactions; simultaneous self- and hetero-association
- Kinetics of binding, aggregation or dissociation over time scales of seconds to hours
CG-MALS characterizes self- and hetero-association.
CG-MALS works by mixing different compositions of samples and diluents, then measuring the weight-average molar mass of the solution at each composition step. Binding kinetics are often apparent.
CG-MALS also characterizes non-specific interactions between proteins at high concentrations and between proteins and excipients, which impact colloidal stability of formulated biotherapeutics. Contact Wyatt to learn how CG-MALS can address your specific biomolecular interaction analyses, such as:
- Drug-target binding for monoclonal antibodies or bispecific fusion proteins
- Monovalent or multi-valent receptors
- Self-association under a variety of buffer conditions
- Multi-protein assemblies in structural biology
- Colloidal stability at protein concentrations of 100 mg/mL and beyond
CG-MALS excels at analyzing multi-protein assemblies.