Sprecher
Beschreibung
An in-line size exclusion chromatography - small-angle neutron scattering (SEC-SANS) setup has been implemented at the KWS-2 instrument at MLZ to enable structural investigations of biomolecules under improved sample quality conditions. By coupling SANS measurements with prior chromatographic separation, challenges associated with sample heterogeneity, aggregation and degradation can be effectively addressed.
The performance of the setup was validated using bovine serum albumin (BSA) as a model protein system containing several oligomeric fractions in solution. The resulting data demonstrate effective chromatographic separation of the targeted monomeric fraction together with simultaneous acquisition of reliable scattering profiles.
Furthermore, BSA in the presence of zwitterionic surfactant sulfobetaine (SB3-12) was investigated as a model protein-surfactant system. The SEC-SANS data show changes in scattering profiles with increasing surfactant concentration, indicating structural rearrangements induced by surfactant binding. These measurements demonstrate the capability of the method to selectively obtain scattering from targeted fractions while reducing contributions from coexisting species and aggregates.
Thus, the SEC-SANS setup at KWS-2 expands the possibilities for future biomedical and pharmaceutical research. It is particularly valuable for investigating proteins, therapeutic formulations and complex biomolecular systems where conventional SANS is limited by sample heterogeneity, tendency to aggregation, or degradation.