Molecular crowding: the history and development of a scientific paradigm

C. Alfano, Y. Fichou, K. Huber, M. Weiss, E. Spruijt, S. Ebbinghaus, G. De Luca, M. A. Morando, V. Verti, P. Temussi*, A. Pastore*

Chemical Reviews, 2024, DOI: 10.1021/acs.chemrev.3c00615


The emerging role of ATP as a cosolute for biomolecular processes

A. Hautke, S. Ebbinghaus*

Biological Chemistry, 2023, DOI: 10.1515/hsz-2023-0202.

Ethylene glycol energetically disfavours oligomerization of pseudoisocyanine dyestuffs at crowded concentrations

S. Rajput, R. Pollak, K. Huber, S. Ebbinghaus, D. Nayar*

Soft Matter, 2023, DOI: 10.1039/D3SM00564J.

Intracellular spatially-targeted chemical chaperones increase native state stability of mutant SOD1 barrel

S. Ribeiro, D. Gnutt, S. Azoulay-Ginsburg, Z. Fetahaj, E. Spurlock, F. Lindner, D. Kuz, Y. Cohen-Erez, H. Rapaport, A. Israelson, A. Gruzman*, S. Ebbinghaus*

Biological Chemistry, 2023, DOI: 10.1515/hsz-2023-0198.

A Comparative Study on Cyanine Dyestuffs as Sensor Candidates for Macromolecular Crowding in Vitro and in Vivo

L. Koch, R. Pollak, S. Ebbinghaus*, K. Huber*

Biosensors, 2023, DOI: 10.3390/bios13070720.

CAG-repeat RNA hairpin folding and recruitment into nuclear speckles with a pivotal role of ATP as a cosolute

A. Hautke, A. Voronin, F. Idiris, A. Riel, F. Lindner, A. Lelièvre, J. Zhu, B. Appel, E. Fatti, K. Weis, S. Mueller, A. Schug, S. Ebbinghaus*

Journal of the American Chemical Society, 2023, DOI: 10.1021/jacs.2c13653.


Superoxide dismutase 1 folding stability as a target for molecular tweezers in SOD1-related amyotrophic lateral sclerosis

N. Samanta#, Y.B. Ruiz-Blanco#, Z. Fetahaj, D. Gnutt, C. Lantz, J.A. Loo, E. Sanchez-Garcia*, S. Ebbinghaus*

ChemBioChem, 2022, DOI: 10.1002/cbic.202200396.

4-Phenylbutyric Acid (4-PBA) Derivatives Prevent SOD1 Amyloid Aggregation In Vitro with No Effect on Disease Progression in SOD1-ALS Mice

L. Alfahel#, S. Argueti-Ostrovsky#, S. Barel#, M. A. Saleh, J. Kahn, S. Azoulay-Ginsburg, A. Rothstein, S. Ebbinghaus, A. Gruzman, A. Israelson*

International Journal of Molecular Science, 2022, DOI: 10.3390/ijms23169403.

A biosensor of protein foldedness identifies increased "holdase" activity of chaperones in the nucleus following increased cytosolic protein aggregation

C. B. Raeburn#, A. R. Ormsby#, D. Cox#, C. A. Gerak, C. Makhoul, N. S. Moily, S. Ebbinghaus, A. Dickson, G. McColl, D. M. Hatters*

Journal of Biological Chemistry, 2022, DOI: 10.1016/j.jbc.2022.102158.

Spatial distribution of intracellular ion concentrations in aggregate forming HeLa cells analyzed by µ-XRF imaging

A. Gräfenstein, C. Rumancev, R. Pollak, B. Hämisch, V. Galbierz, W. H. Schröder, J. Garrevoet, G. Falkenberg, T. Vöpel, K. Huber, S. Ebbinghaus*, A. Rosenhahn*

Chemistry Open, 2022, DOI: 10.1002/open.202200024.

Disease-related protein variants of the highly conserved enzyme PAPSS2 show marginal stability and aggregation in cells

O. Brylski#, P. Shrestha#, P. J. House, P. Gnutt, J. Wolf Mueller*, S. Ebbinghaus*

Frontiers Molecular Biosciences, 2022, DOI: 10.3389/fmolb.2022.860387.


Cellular ATP levels determine the stability of a nucleotide kinase

O. Brylski, P. Shrestha, P. Gnutt, D. Gnutt, J. Wolf Mueller*, S. Ebbinghaus*

Frontiers in Molecular Biosciences, 2021, DOI: 10.3389/fmolb.2021.790304.

Sequestration of Proteins in Stress Granules Relies on the In-Cell but Not the In Vitro Folding Stability

N. Samanta#, S. S. Ribeiro#, M. Becker, E. Laborie, R. Pollak, S. Timr*, F. Sterpone*, S. Ebbinghaus*

Journal of the American Chemical Society, 2021, DOI: 10.1021/jacs.1c09589.

GlycoBODIPYs: Sugars Serving as Natural Stock for Water-soluble Flourescent Probes of Complex Chiral Morphology

L. J. Patalag*#, S. Ahadi#, O. Lashchuk, P. G. Jones, S. Ebbinghaus, D. B. Werz*

Angewandte Chemie, International Edition, 2021, DOI: 10.1002/anie.202016764.

Chemical Chaperons Targeted to ER and lysosome Chemical Charperones Prevented Neurodegeneration in C9orf72 Repeat Expansion Drosophila ALS Model

S. Azoulay-Ginsburg#, M. Di Salvio, M. Weitman, M. Afri, S. Ribeiro, S. Ebbinghaus, G. Cestra, A. Gruzman*

Pharmacological Reports, 2021, DOI: 10.1007/s43440-021-00226-2.

Micro-XRF analysis of trace element distribution in frozen hydrated HeLa cells at the P06 beamline at Petra III

C. Rumancev, T. Vöpel, S. Stuhr, A. R. von Gundlach, T. Senkbeil, S. Ebbinghaus, J. Garrevoet, G. Falkenberg, B. De Samber, L. Vincze, A. Rosenhahn*, W. Schröder*

Biointerphases, 2021, DOI: 10.1116/6.0000593.

Thermodynamic Analysis of the Self-Assembly of Pseudo Isocyanine Chloride in the Presence of Crowding Agents

B. Hämisch, R. Pollak, S. Ebbinghaus*, K. Huber*

ChemSystemsChem, 2021, DOI: 10.1002/syst.202000051.


Folding stability and self‐association of a triplet‐repeat (CAG)_20 RNA hairpin in cytomimetic media

A. C. Hautke, S. Ebbinghaus*

ChemSystemsChem, 2020, DOI: 10.1002/syst.202000052.

In cellulo analysis of Huntingtin inclusion bodies by cryogenic nanoprobe SAXS

C. Rumancev*, T. Vöpel, S. Stuhr, A. von Gundlach, T. Senkbeil, M. Osterhoff, M. Sprung, V. Garamus, S. Ebbinghaus*, A. Rosenhahn*

ChemSystemsChem, 2020, DOI: 10.1002/syst.202000050.

The Unfolding Journey of Superoxide Dismutase 1 Barrels Under Crowding: Atomistic Simulations Shed Light on Intermediate States and Their Interactions With Crowders

S. Timr*, D. Gnutt, S. Ebbinghaus, F. Sterpone*

The Journal of Physical Chemistry Letters, 2020, DOI: 10.1021/acs.jpclett.0c00699.

Self‐Assembly of Pseudo‐Isocyanine Chloride as a Sensor for Macromolecular Crowding in vitro and in vivo

B. Hämisch#, R. Pollak#, S. Ebbinghaus*, K. Huber*

Chemistry - A European Journal, 2020, DOI: 10.1002/chem.202000113.

X-ray fluorescence analysis of metal distributions in cryogenic biological samples using large-acceptance-angle SDD detection and continuous scanning at the Hard X-ray Micro/Nano-Probe beamline P06 at PETRA III

C. Rumancev#, A. Gräfenstein#, T. Vöpel, S. Stuhr, A. R. von Gundlach, T. Senkbeil, J. Garrevoet, L. Jolmes, B. König, G. Falkenberg, S. Ebbinghaus, W. H. Schroeder, A. Rosenhahn*

Journal of Synchrotron Radiation, 2020, DOI: 10.1107/S1600577519014048.

Thermal Stability Modulation of Native and Chemically-Unfolded State of Bovine Serum Albumin by Amino Acids

S. Pal, P. Pyne, N. Samanta, S. Ebbinghaus*, R. K. Mitra*

Physical Chemistry Chemical Physics, 2020, DOI: 10.1039/C9CP04887A.


The synergic effect of water and biomolecules in intracellular phase separation

S. S. Ribeiro, N. Samanta, S. Ebbinghaus, J. C. Marcos*

Nature Reviews Chemistry, 2019, DOI: 10.1038/s41570-019-0120-4.

Effects of in vivo conditions on amyloid aggregation

M.C. Owen#, D. Gnutt#, M. Gao#, S. Warmländer, J. Jarvet, A. Gräslund, R. Winter, S. Ebbinghaus, B. Strodel*

Chemical Society Reviews, 2019, DOI: 10.1039/C8CS00034D.

Protein Folding Modulation in Cells Subject to Differentiation and Stress

D. Gnutt, L. Sistemich, S. Ebbinghaus*

Frontiers in Molecular Biosciences, 2019, DOI: 10.3389/fmolb.2019.00038.

Melting Down Protein Stability: PAPS Synthase 2 in Patients and in a Cellular Environment

O. Brylski, S. Ebbinghaus, J.W. Mueller*

Frontiers in Molecular Biosciences, 2019, DOI: 10.3389/fmolb.2019.00031.

Stability Effect of Quinary Interactions Reversed by Single Point Mutations

D. Gnutt, S. Timr, J. Ahlers, B. König, E. Manderfeld, M. Heyden, F. Sterpone, S. Ebbinghaus*

Journal of the American Chemical Society, 2019, DOI: 10.1021/jacs.8b13025.


Protein folding and quinary interactions: Creating cellular organization through functional disorder

S.S. Ribeiro, S. Ebbinghaus, J.C. Marcos*

FEBS Letters, 2018, DOI: 10.1002/1873-3468.13211.

Macromolecular crowding effects in flexible polymer solutions

B.B. Majumdar, S. Ebbinghaus, M.Heyden*

Journal of Theoretical and Computational Chemistry, 2018, DOI: 10.1142/S0219633618400060.

A biosensor-based framework to measure latent proteostasis capacity

R.J. Wood, A.R. Ormsby, M. Radwan, D. Cox, A. Sharma, T. Vöpel, S. Ebbinghaus, M. Oliveberg, G.E. Reid, A. Dickson, D.M. Hatters*

Nature Communications, 2018, DOI: 10.1038/s41467-017-02562-5 .

A multi-perspective approach to solvent regulation of enzymatic activity: HMG-CoA reductase

M. Dirkmann, J. Iglesias, V. Muñoz, P. Sokkar, C. Rumancev, A. von Gundlach, O. Krenczyk, T. Vöpel, J. Nowack, M. A. Schroer, S. Ebbinghaus, C. Herrmann, A. Rosenhahn, E. Sanchez-Garcia* and F. Schulz*

ChemBioChem, 2018, DOI: 10.1002/cbic.201700596.


Imperfect crowding adaptation of mammalian cells towards osmotic stress and its modulation by osmolytes

D. Gnutt, O. Brylski, E. Edengeiser, M. Havenith, S. Ebbinghaus*

Molecular BioSystems, 2017, DOI: 10.1039/c9sc00749k.

Elucidation of the Catalytic Mechanism of a Miniature Zinc Finger Hydrolase

A. Ganguly, T. Luong, O. Brylski, M. Dirkmann, D. Möller, S. Ebbinghaus, F. Schulz, R. Winter, E. Sanchez-Garcia*, W. Thiel*

Journal of Physical Chemistry B, 2017, DOI: 10.1021/acs.jpcb.7b05027.

Inhibition of Huntingtin Exon‑1 Aggregation by the Molecular Tweezer CLR01

T. Vöpel, K. Bravo-Rodriguez, S. Mittal, S. Vachharajani, D. Gnutt, A. Sharma, A. Steinhof, O. Fatoba, G. Ellrichmann, M. Nshanian, C. Heid, J. A. Loo, F. G. Klärner, T. Schrader, G. Bitan, E. E. Wanker, S. Ebbinghaus*, E. Sanchez-Garcia*

Journal of the American Chemical Society, 2017, DOI: 10.1021/jacs.6b11039.

Conformational dynamics and self-association of intrinsically disordered Huntingtin exon 1 in cells

S. Büning, A. Sharma, S. Vachharajani, E. Newcombe, A. Ormsby, M. Gao, D. Gnutt, T. Vöpel, D. M. Hatters, S. Ebbinghaus*

Physical Chemistry Chemical Physics, 2017, DOI: 10.1039/C6CP08167C.

Das Innere der Zelle: Ein komplexes Lösungsmittel

M. Heyden, S. Ebbinghaus, R. Winter*

Chemie in unserer Zeit, 2017, DOI: 10.1002/ciuz.201700777.


The Temperature Dependence of the Hofmeister Series: Thermodynamic Fingerprints of Cosolute-Protein Interactions

M. Senske, D. Constantinescu, M. Havenith, C. Herrmann*, H. Weingärtner, S. Ebbinghaus*

Physical Chemistry Chemical Physics, 2016, DOI: 10.1039/C6CP05080H.

RNA hairpin folding in the crowded cell

M. Gao#, D. Gnutt#, A. Orban, B. Appel, F. Righetti, R. Winter, F. Narberhaus, S. Müller, S. Ebbinghaus*

Angewandte Chemie, International Edition, 2016, DOI: 10.1002/anie.201510847.

Simultaneous measurements of photocurrents and H2O2 evolution from solvent exposed Photosystem 2 complexes

T. Vöpel, E.N. Saw, V. Hartmann, R. Williams, F. Müller, W. Schuhmann, N. Plumeré, M. Nowaczyk, S. Ebbinghaus*, M. Rögner*

Biointerphases, 2016, DOI: 10.1116/1.4938090.

Vom Reagenzglas in die Zelle

D. Gnutt, M. Heyden* and S. Ebbinghaus*

Nachrichten aus der Chemie (Trendbericht Physikalische Chemie), 2016, DOI: 10.1002/nadc.20164047296.

The macromolecular crowding effect – from in vitro into the cell

D. Gnutt and S. Ebbinghaus*

Biological Chemistry, 2016, DOI: 10.1515/hsz-2015-0161.

Protein stability in crowded environments

M. Senske, S. Ebbinghaus and C. Herrmann*

Book chapter in Biocalorimetry: Foundations and Contemporary Approaches (Taylor & Francis), 2016, DOI: 10.1201/b20161.


Infrared laser triggered release of bioactive compounds from single hard shell microcapsules

T. Vöpel, R. Scholz, L. Davico, M. Groß, S. Büning, S. Kareth, E. Weidner and S. Ebbinghaus*

Chemical Communications, 2015, DOI: 10.1039/C4CC09745A.

Excluded volume effects in the living cell

D. Gnutt, M. Gao, O. Brylski, M. Heyden and S.Ebbinghaus*

Angewandte Chemie, International Edition, 2015, DOI: 10.1002/anie.201409847.

Modulation of human IAPP fibrillation: Cosolutes, crowders and chaperones

M. Gao, K. Estel, J. Seeliger, R.P. Friedrich, S. Dogan, E.E. Wanker, R. Winter and S. Ebbinghaus*

Physical Chemistry Chemical Physics, 2015, DOI: 10.1039/C4CP04682J

Non-invasive chemical assessment of living human spermatozoa

E. Edengeiser, K. Meister, E. Bründermann, S. Büning, S. Ebbinghaus, M. Havenith*

RSC Advances, 2015, DOI: 10.1039/C4RA12158A.

Understanding the 'native' solvent – from the test tube into the cell

M. Senske, S. Büning and S. Ebbinghaus*

Bunsenmagazin, (6), 276-281, 2014.

Protein Stabilization by Macromolecular Crowding through Enthalpy rather than Entropy

M. Senske, L. Törk, B. Born, M. Havenith, C. Herrmann and S. Ebbinghaus*

Journal of the American Chemical Society, 2014, DOI: 10.1021/ja503205y.

Relaxationskinetik in lebenden Zellen

S. Büning, S. Ebbinghaus*

BIOspektrum, 20(4), 383-385, 2014.

Particle Dynamics Microscopy Using Temperature Jump and Probe Anticorrelation/Correlation Techniques

M. Gruebele, S. Ebbinghaus, A. Dhar, J. D. McDonald 

US patent 8,757,871, 2014.

Probing solvation dynamics by THz absorption spectroscopy

B. Born, M. Heyden, S. Ebbinghaus and M. Havenith*

Terahertz Biomedical Science and Technology, CRC Press, 2014, ISBN: 9780429194283.

Long-range protein-water dynamics in hyperactive insect antifreeze proteins

K. Meister, S. Ebbinghaus, Y. Xu, J.G. Duman, A.L. DeVries, M. Gruebele, D.M. Leitner and M. Havenith*

Proceedings of the National Academy of Sciences of the United States of America, 2013, DOI: 10.1073/pnas.1214911110.

"How An Insect Version Of Antifreeze Works" Veröffentlichung in Chemical & Engineering News

Functional Importance of Short-Range Binding and Long-Range Solvent Interactions in Helical Antifreeze Peptides

S. Ebbinghaus, K. Meister, M. B. Prigozhin, A. L. DeVries, M. Havenith, J. Dzubiella, and M. Gruebele*

Biophysical Journal, 2012, DOI: 10.1016/j.bpj.2012.06.013.

Protein Stability and Folding Kinetics in the Nucleus and Endoplasmic Reticulum of Eucaryotic Cells

A. Dhar, K. Girdhar, D. Singh, H. Gelman, S. Ebbinghaus, M. Gruebele*

Biophysical Journal, 2011, DOI: 10.1016/j.bpj.2011.05.071.

Protein Folding Landscapes in the Living Cell

S. Ebbinghaus and M. Gruebele*

Journal of Physical Chemistry Letters, 2011, DOI: 10.1021/jz101729z.


Structure, function, and folding of phosphoglycerate kinase are strongly perturbed by macromolecular crowding

A. Dhar, A. Samiotakis, S. Ebbinghaus, L. Nienhaus, D. Homouz, M. Gruebele, M.S. Cheung*

Proceedings of the National Academy of Sciences of the United States of America , 2010, DOI: 10.1073/pnas.1006760107.

The diffusion coefficient for PGK folding in eukaryotic cells

A. Dhar#, S. Ebbinghaus#, Z. Shen, T. Mishra, M. Gruebele*

Biophysical Journal, 2010, DOI: 10.1016/j.bpj.2010.08.066.

Antifreeze glycoprotein activity correlates with long-range protein-water dynamics

S. Ebbinghaus, K. Meister, B. Born, A. L. DeVries, M. Gruebele and M. Havenith*

Journal of the American Chemical Society, 2010, DOI: 10.1021/ja1051632.

Terahertz Spectroscopy as a Tool to Study Hydration Dynamics

M. Heyden, S. Ebbinghaus, M. Havenith*

Encyclopedia of Analytical Chemistry, 2010, DOI: 10.1002/9780470027318.a9162.

Protein folding stability and dynamics imaged in a living cell

S. Ebbinghaus, A. Dhar, J.D. McDonald and M. Gruebele*

Nature Methods, 2010, DOI: 10.1038/nmeth.1435.

Protein folding stability and The terahertz dance of water with the proteins: the effect of protein flexibility on the dynamical hydration shell of ubiquitinimaged in a living cell

B. Born, S.J. Kim, S. Ebbinghaus, M. Gruebele, M. Havenith*

Faraday Discussions, 2009, DOI: 10.1039/b804734k.

Protein sequence- and pH-dependent hydration probed by Terahertz spectroscopy

S. Ebbinghaus, S.J. Kim, M. Heyden, X. Yu, M. Gruebele, D. Leitner and M. Havenith*

Journal of the American Chemical Society, 2008, DOI: 10.1021/ja0746520.

An extended dynamical solvation shell around proteins

S. Ebbinghaus, S.J. Kim, M. Heyden, X. Yu, U. Heugen, M. Gruebele, D. Leitner and M. Havenith*

Proceedings of the National Academy of Sciences of the United States of America, 2007, DOI: 10.1073/pnas.0709207104.

Terahertz time-domain spectroscopy as a new tool for the characterization of dust forming plasmas

S. Ebbinghaus, K. Schröck, J.C. Schauer, E. Bründermann, M. Heyden, G. Schwaab, M. Böke, J. Winter, M. Tani and M. Havenith*

Plasma Sources Science and Technology, 2006, DOI: 10.1088/0963-0252/15/1/011.

Terahertz Imaging Applications in Spectroscopy of Biomolecules

E. Bründermann, U. Heugen, R. Schiwon, B. Born, G.W. Schwaab, S. Ebbinghaus, K. Schröck, D.R. Chamberlin, E.E. Haller and M. Havenith*

IEEE MTT-S International Microwave Symposium Digest, 2005, DOI: 10.1109/MWSYM.2005.1516679.

High resolution spectroscopy of the ν3 band of DCOOD

F. Madeja, A. Hecker, S. Ebbinghaus and M. Havenith*

Spectrochimica Acta Part A, 2003, DOI: 10.1016/S1386-1425(02)00412-2.

High resolution spectroscopy of the ν3 band of the van der Waals complex Ar-DCOOH

F. Madeja, A. Hecker, S. Ebbinghaus and M. Havenith*

Molecular Physics, 2003, DOI: 10.1080/0026897031000108078.