Publications by authors named "J Anzengruber"
Purpose: To explore how the natural heterogeneity of human coagulation factor VIII (FVIII) and the processing of its B-domain specifically modulate protein aggregation.
Methods: Recombinant FVIII (rFVIII) molecular species containing 70% or 20% B-domain, and B-domain-deleted rFVIII (BDD-rFVIII), were separated from full-length recombinant FVIII (FL-rFVIII). Purified human plasma-derived FVIII (pdFVIII) was used as a comparator.
Unlabelled: Essentials Glycosylation heterogeneity of recombinant proteins affects pharmacokinetics and immunogenicity. N-glycomics/glycoproteomics of plasma-derived Factor VIII and 6 recombinant FVIIIs were compared. Depending on cell line, significant differences to plasma-derived FVIII were observed.
View Article and Find Full Text PDFUnlabelled: Essentials Aggregation is a critical quality attribute of protein therapeutics influencing immunogenicity. Aggregates and subvisible particles in 9 recombinant factor VIII (rFVIII) products were analyzed. Major differences in aggregate and particle concentrations were detected after reconstitution.
View Article and Find Full Text PDFArticle Synopsis
- Lactobacillus buchneri CD034 has a unique two-dimensional S-layer on its surface, but understanding how this layer connects to the cell wall is still unclear.
- Researchers identified lipoteichoic acid as a key component of the bacterium's cell wall, which may play a role in this binding process.
- The study used advanced techniques like NMR and single-molecule force spectroscopy to reveal that the S-layer protein and lipoteichoic acid directly interact, providing insights into the structural integrity of Lactobacillus cell walls.