Medizinische Universität Graz Austria/Österreich - Forschungsportal - Medical University of Graz

Logo MUG-Forschungsportal

Gewählte Publikation:

SHR Neuro Krebs Kardio Lipid Stoffw Microb

Zhang, F; Richter, G; Bourgeois, B; Spreitzer, E; Moser, A; Keilbach, A; Kotnik, P; Madl, T.
A General Small-Angle X-ray Scattering-Based Screening Protocol for Studying Physical Stability of Protein Formulations.
Pharmaceutics. 2021; 14(1): Doi: 10.3390/pharmaceutics14010069 [OPEN ACCESS]
Web of Science PubMed PUBMED Central FullText FullText_MUG


Führende Autor*innen der Med Uni Graz
Madl Tobias
Zhang Fangrong
Co-Autor*innen der Med Uni Graz
Bourgeois Benjamin Michel Rene
Richter Gesa Lucia
Spreitzer Emil

Dimensions Citations:

Plum Analytics:

Scite (citation analytics):

A fundamental step in developing a protein drug is the selection of a stable storage formulation that ensures efficacy of the drug and inhibits physiochemical degradation or aggregation. Here, we designed and evaluated a general workflow for screening of protein formulations based on small-angle X-ray scattering (SAXS). Our SAXS pipeline combines automated sample handling, temperature control, and fast data analysis and provides protein particle interaction information. SAXS, together with different methods including turbidity analysis, dynamic light scattering (DLS), and SDS-PAGE measurements, were used to obtain different parameters to provide high throughput screenings. Using a set of model proteins and biopharmaceuticals, we show that SAXS is complementary to dynamic light scattering (DLS), which is widely used in biopharmaceutical research and industry. We found that, compared to DLS, SAXS can provide a more sensitive measure for protein particle interactions, such as protein aggregation and repulsion. Moreover, we show that SAXS is compatible with a broader range of buffers, excipients, and protein concentrations and that in situ SAXS provides a sensitive measure for long-term protein stability. This workflow can enable future high-throughput analysis of proteins and biopharmaceuticals and can be integrated with well-established complementary physicochemical analysis pipelines in (biopharmaceutical) research and industry.

Find related publications in this database (Keywords)
© Med Uni Graz Impressum