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Dr. rer. nat., Physical Biology, Heinrich Heine University Düsseldorf, Germany, 2015
Diploma, Pharmacy, University Greifswald, Germany, 2010
Association and aggregation play an important role in development of pharmaceutical peptide formulations. A detailed understanding about solvent dependent changes in the association state is an essential tool. These information are relevant for development of stable storage formulations or predictions of the peptide behavior after patient treatment. To analyze peptide association and peptide interactions we combine several hydrodynamic and spectroscopic methods, e.g. static (SLS) and dynamic (DLS) light scattering, circular dichroism spectroscopy and fluorescence spectroscopy.
Bremer A, Wolff M, Thalhammer A, Hincha DK. Folding of intrinsically disordered plant LEA proteins is driven by glycerol-induced crowding and the presence of membranes. FEBS J. 2017
Wolff M, Unuchek D, Zhang B, Gordeliy V, Willbold D, Nagel-Steger L. Amyloid beta Oligomeric Species Present in the Lag Phase of Amyloid Formation. PLoS One. 2015
Gruning CS, Klinker S, Wolff M, Schneider M, Toksoz K, Klein AN, et al. The off-rate of monomers dissociating from amyloid-beta protofibrils. J Biol Chem. 2013
Luers L, Bannach O, Stohr J, Wordehoff MM, Wolff M, Nagel-Steger L, et al. Seeded fibrillation as molecular basis of the species barrier in human prion diseases. PLoS One. 2013
I have given lectures and practical courses in Düsseldorf and Potsdam in the field of Physical Biology.