Alumni Ebbinghaus publishes new research on Macromolecular crowding effect



A central dogma in crowding theories was that crowding effects are solely mediated by hard-core repulsions between the macromolecules and therefore steric excluded volume effects. This ideal excluded volume effect would result in an entropic stabilization of a protein while the enthalpy remains unchanged. However, using artificial crowding agents like Ficoll 70 former CPLC fellow Simon Ebbinghaus and his students Michael Senske and David Gnutt have recently shown that crowding effects on protein stability can be primarily mediated by enthalpic effects (1). In the cellular environment, excluded volume effects are further compensated by unspecific interactions (2). However, hypertonic stress can evoke significant excluded volume effects that lead to high compression forces acting on biomolecules in cells (2). Such effects could endanger proteostasis and promote protein aggregation.

Simon Ebbinghaus has been a Assistent Professor at the Ruhr-University Bochum (Department of Physical Chemistry II) since 2011. Before that, he worked as a Feodor Lynen and CPLC Fellow with Martin Gruebele at the University of Illinois (Urbana-Champaign) from 2008 to 2010. For more details, see



(1) M. Senske, L. Törk, B. Born, M. Havenith, C. Herrmann, S. Ebbinghaus. Protein Stabilization by Macromolecular Crowding through Enthalpy rather than Entropy. J. Am. Chem. Soc., 136(25): 9036–9041, 2014.

(2) D. Gnutt, M. Gao, O. Brylski, M. Heyden and S. Ebbinghaus. Excluded volume effects in the living cell. Angew. Chem. Int. Ed., Accepted Manuscript, DOI: 10.1002/anie.201409847R1