Wyatt Technology

Live Webinars

For Effective Protein Quality Control and Aggregate Detection, Couple SEC to Multi-Angle Light Scattering (SEC-MALS)

Join us for a webinar on February 16th at 14:30 CET | 8:30 AM EST

Protein science as well as the exploration of other biomolecules has made an enormous development over recent years. Especially antibodies and similar therapeutic proteins are utilized for diagnostics and therapy on an unprecedented scale. But antibodies and other proteins are prone to forming oligomers and aggregates, which can be the bottleneck in preparation. In this webinar we present how Multi-Angle Light Scattering coupled to size exclusion chromatography (SEC MALS) can be used to check protein preparations for aggregates and sample stability. Application examples will show how this technique can help to improve protein cleaning and optimize protein formulation.

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Vision of a New Separation Method for Macromolecules and Nanoparticles: Flow FFF with Electrical Field

Join us for a webinar on February 28th at 14:30 CET | 8:30 AM EST

Electrical Field-Flow Fractionation (EAF4) is a new FFF separation method in which an electrical field is employed in addition and parallel to the flow field of the asymmetric flow field flow fractionation (AF4). Under the influence of the electrical field the retention time of the eluting species can be shifted according to their electrophoretic mobility. Therefore EAF4 can be used to determine the absolute value of electrophoretic mobility and its distribution for a sample. The application of EAF4 is shown for colloidal drug carriers which are designed to transport a paid load (RNA or DNA) to the cell or the cell nucleus.

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Analyzing Ebola virus glycoprotein and its interactions with therapeutic antibodies using CG-MALS

Join us for a webinar on March 15th at 8:00 AM PST | 11:00 AM EST | 4:00 PM CET

The Ebolavirus (EBOV) glycoprotein (GP) is essential for the attachment and fusion of virus and host cell membranes. It is also the primary target of neutralizing and therapeutic antibody responses. EBOV GP is found as a trimeric complex on the viral surface. Whether multiple antibodies bind to these complexes and with what affinity is critical information when designing vaccines or creating a post-exposure antibody treatments.
Using composition-gradient multi-angle light scattering (CG-MALS), which quantifies the change in apparent weight-average molar mass (Mw) as a function of composition, we analyzed the reversible association between EBOV GP and antibodies that are neutralizing or protective. This technique enabled determination of the affinity and stoichiometry of various immune complexes as well as the relative quantity of each type of complex. The best-fit model determined from the CG-MALS data was supported by structural characterization using cryo-EM (Pallesen, et al. Nature Microbiology, 2016).
This webcast will include an introduction to SEC-MALS and CG-MALS as absolute biophysical characterization methods, then explain how we characterize the glycan content and oligomerization state of EBOV GP using SEC-MALS. We then demonstrate the detailed information we can gain about GP-antibody interactions using CG-MALS. The webcast will also address practical issues such as the preparation of proteins for light-scattering studies, setup of the instruments, analysis of the data and critical evaluation of the results.

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Wyatt Technology is the recognized leader in light scattering instrumentation and software for determining the absolute molar mass, size, charge and interactions of macromolecules and nanoparticles in solution.

Wyatt's line of multi-angle static light scattering products couple to size exclusion chromatography (SEC-MALS), field-flow fractionation (FFF-MALS), and stop-flow composition-gradient systems (CG-MALS). Our dynamic light scattering (DLS) products operate in traditional cuvette as well as on-line and automated, high-throughput modes. We also offer unique instruments for electrophoretic light scattering (MP-PALS), differential refractometry, and differential viscosity.



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