Research: Amyloid biotechnology

Amyloid fibrils may not only occur inside living organismus in the course of disease, but also as functional devices. Likewise there are increasing attempts to utilize amyloids for technological purposes. We previously extended this research by analyzing the applicative potential of amyloid oligomers. Moreover, we have been using biotechnologically engineered antibody fragments to investigate the mechanism and pathogenicity of different amyloid structures.

Photo shows the structure of amyloid fibrils


Selected references:

Luong TQ, Erwin N, Neumann M, Schmidt A, Loos C, Schmidt V, Fändrich M, Winter R
Hydrostatic pressure increases the catalytic activity of amyloid fibril enzymes.
Angewandte Chemie Int. Ed. 2016, 55, 12412–12416

Aumüller T, Fändrich M
Protein chemistry: Catalytic amyloid fibrils.
Nature Chemistry 2014, 6, 273-274

Kumar ST, Meinhardt J, Fuchs AK, Aumüller T, Leppert J, Büchele B, Knüpfer U, Ramachandran R, Yadav JK, Prell E, Morgado I, Ohlenschläger O, Horn U, Simmet T, Görlach M, Fändrich M
Structure and biomedical applications of amyloid oligomer nanoparticles.
ACS Nano 2014, 25, 8, 11042-11052

 

Contact

Prof. Dr. Marcus Fändrich
Tel: +49-(0)731/50 32750
Fax: +49-(0)731/50 32759
E-Mail: marcus.faendrich
Helmholtzstraße 8/1
Room number 1.55