Protein biotechnology provides a crucial basis to investigate amyloidogenic proteins and their derived amyloid states. For example, we previously have been using biotechnologically engineered antibody fragments to investigate the mechanism and pathogenicity of different amyloid structures. To that end, we have set up bacterial high cell density fermentation in bioreactors for recombinant protein production. Furthermore, we use a battery of modern high flow rate FPLC systems to purify proteins from small scale to bioprocess scale.

Selected references:

Haupt C, Fändrich M
Biotechnologically engineered protein binders for applications in amyloid diseases.
Trends Biotechnol. 2014, 32, 513-520

Morgado I, Wieligmann K, Bereza M, Rönicke R, Meinhardt K, Wacker J, Hortschansky P, Malešević M, Parthier C, Schiene-Fischer C, Reymann KG, Stubbs MT, Görlach M, Horn U, Fändrich M
Molecular Basis of β-Amyloid Oligomer Binding and Inhibition with a Conformation-Specific Antibody Fragment.
Proc. Natl. Acad. Sci. U.S.A. 2012, 109, 12503-12508

Habicht G, Haupt C, Friedrich RP, Hortschansky P, Sachse C, Meinhardt J, Wieligmann K, Gellermann GP, Brodhun M, Götz J, Halbhuber KJ, Röcken C, Horn U, Fändrich M
Directed selection of a conformational antibody domain that prevents mature amyloid fibril formation by stabilizing Ab protofibrils.
Proc. Natl. Acad. Sci. U.S.A. 2007, 104, 19232-19237

Hortschansky P, Schroeckh V, Christopeit T, Zandomeneghi G, Fändrich M
The aggregation kinetics of Alzheimer's ß-amyloid peptide is controlled by stochastic nucleation.
Protein Sci. 2005, 14, 1753-1759