Multimeranalyse

Multimeranalyse is a set of analytical methods used to characterize multimeric macromolecular assemblies, focusing on oligomeric state, stoichiometry, assembly and disassembly pathways, subunit interactions, and stability under defined conditions. The approach is used across biochemistry, structural biology, and pharmaceutical sciences to study protein complexes, antibody systems, virus-like particles, and nucleic acid–protein assemblies.

A range of techniques is commonly employed, often in combination. Size-exclusion chromatography coupled to multi-angle light scattering (SEC-MALS) provides molecular weight and oligomeric state in solution. Analytical ultracentrifugation, including sedimentation velocity and sedimentation equilibrium, yields size, shape, and stoichiometry information. Native mass spectrometry preserves noncovalent assemblies for direct mass measurement. Dynamic light scattering (DLS) gives hydrodynamic size and sample homogeneity. Small-angle X-ray or neutron scattering (SAXS/SANS) reports on overall shape and assembly in solution. Cross-linking mass spectrometry, cryo-electron microscopy (cryo-EM) and single-particle analysis offer structural details. Other supportive methods include native gel-based assays and various spectroscopic techniques sensitive to oligomerization.

Applications of multimeranalyse include characterizing the oligomeric states of enzymes and signaling proteins, analyzing protein–protein interactions, evaluating engineered multimeric constructs, and quality control for biologics such as therapeutic antibodies and viral vectors. It supports formulation development, stability assessment, and mechanistic studies of assembly processes.

Limitations arise from dynamic equilibria, concentration-dependent dissociation, and potential disruption of weak interactions during measurement. Reliable interpretation often requires orthogonal methods, careful maintenance of near-native conditions, and corroborating data across multiple techniques.