Publications

2025

Dreier JE, Stevenson A, Carles E, Schott K, Michaels TCT, Galvagnion C. Ambroxol displaces α-synuclein from the membrane and inhibits the formation of early protein-lipid coaggregates. Chem Sci. 2025 Oct 31. doi: 10.1039/d5sc06116d.

Stevenson A, Staats R, Dear AJ, Voderholzer D, Dreier JE, Meisl G, Guido R, Knowles TPJ, Galvagnion C, Buell AK, Vendruscolo M, Michaels TCT. Global kinetic model of lipid-induced α-synuclein aggregation and its inhibition by small molecules. Proc Natl Acad Sci U S A. 2025 Jul;122(26):e2422427122. https://doi.org/10.1073/pnas.2422427122.

2024

Galvagnion, C., Barclay, A., Makasewicz, K., Marlet, F.R., Moulin, M., Devos, J., et al. (2024). Structural characterisation of α-synuclein-membrane interactions and the resulting aggregation using small angle scattering. Physical chemistry chemical physics, 14. https://doi.org/10.1039/d3cp05928f

Marlet, FR, Muñoz, SS, Sotiraki, N, Eliasen, JN, Woessmann, J, Weicher, J, Dreier, JE, Schoof, E, Kohlmeier, KA, Maeda, K, Galvagnion, C. Lipid levels correlate with neuronal and dopaminergic markers during the differentiation of SH-SY5Y cells. Biochimica et Biophysica Acta (BBA) – Molecular Basis of Disease, 13;1870(6):167212. https://doi.org/10.1016/j.bbadis.2024.167212

2022

Vassallo, N., Galvagnion, C., & Chi, E. Y. (2022). Editorial: Amyloid-membrane interactions in protein misfolding disorders: From basic mechanisms to therapy. Frontiers in Cell and Developmental Biology, 10:870791. https://doi.org/10.3389/fcell.2022.870791

Bell, R., Thrush, R. J., Castellana-Cruz, M., Oeller, M., Staats, R., Nene, A., Flagmeier, P., Xu, C. K., Satapathy, S., Galvagnion, C., Wilson, M. R., Dobson, C. M., Kumita, J. R., & Vendruscolo, M. (2022). N-terminal acetylation of α-synuclein slows down its aggregation process and alters the morphology of the resulting aggregates. Biochemistry, 61(17), 1743–1756. https://doi.org/10.1021/acs.biochem.2c00104

Galvagnion, C., Marlet, F. R., Cerri, S., Schapira, A. H. V., Blandini, F., & Di Monte, D. A. (2022). Sphingolipid changes in Parkinson L444P GBA mutation fibroblasts promote α-synuclein aggregation. Brain, 145(3), 1038–1051. https://doi.org/10.1093/brain/awab371

2021

Stender, E. G., Ray, S., Norrild, R. K., Larsen, J. A., Petersen, D., Farzadfard, A., Galvagnion, C., Jensen, H., & Buell, A. K. (2021). Capillary flow experiments for thermodynamic and kinetic characterization of protein liquid-liquid phase separation. Nature Communications, 12(1). https://doi.org/10.1038/s41467-021-27433-y

Muñoz, S. S., Petersen, D., Marlet, F. R., Kücükköse, E., & Galvagnion, C. (2021). The interplay between Glucocerebrosidase, α-synuclein and lipids in human models of Parkinson’s disease. Biophysical Chemistry, 273. https://doi.org/10.1016/j.bpc.2020.106534

2019

Galvagnion, C., Topgaard, D., Makasewicz, K., Buell, A. K., Linse, S., Sparr, E., & Dobson, C. M. (2019). Lipid Dynamics and Phase Transition within α-Synuclein Amyloid Fibrils. The Journal of Physical Chemistry Letters, 10(24), 7872-7877. https://doi.org/10.1021/acs.jpclett.9b03299

Agerschou, E. D., Flagmeier, P., Saridaki, T., Galvagnion, C., Komnig, D., Heid, L., Prasad, V., Shaykhalishahi, H., Willbold, D., Dobson, C. M., Voigt, A., Falkenburger, B., Hoyer, W., & Buell, A. K. (2019). An engineered monomer binding-protein for α-synuclein efficiently inhibits the proliferation of amyloid fibrils. eLife, 8. https://doi.org/10.7554/elife.46112

2018

Perni, M., Flagmeier, P., Limbocker, R., Cascella, R., Aprile, F. A., Galvagnion, C., Heller, G. T., Meisl, G., Chen, S. W., Kumita, J. R., Challa, P. K., Kirkegaard, J. B., Cohen, S. I. A., Mannini, B., Barbut, D., Nollen, E. A. A., Cecchi, C., Cremades, N., Knowles, T. P. J., Chiti, F., Zasloff, M., Vendruscolo, M., & Dobson, C. M. (2018). Multistep Inhibition of α-Synuclein Aggregation and Toxicity in Vitro and in Vivo by Trodusquemine. ACS Chemical Biology, 13(8), 2308-2319. doi: 10.1021/acschembio.8b00427

Brown, J. W. P., Meisl, G., Knowles, T. P. J., Buell, A. K., Dobson, C. M., & Galvagnion, C. (2018). Kinetic barriers to α-synuclein protofilament formation and conversion into mature fibrils. Chemical Communications, 54(56), 7854-7857. doi: 10.1039/C8CC04172E

Van der Wateren, I. M., Knowles, T. P. J., Buell, A. K., Dobson, C. M., & Galvagnion, C. (2018). C-terminal truncation of α-synuclein promotes amyloid fibril amplification at physiological pH. Chemical Science, 9(25), 5506-5516. doi: 10.1039/C8SC01925C

Habchi, J., Chia, S., Galvagnion, C., Michaels, T. C. T., Bellaiche, M. M. J., Ruggeri, F. S., Sanguanini, M., Idini, I., Kumita, J. R., Sparr, E., Linse, S., Dobson, C. M., Knowles, T. P. J., & Vendruscolo, M. (2018). Cholesterol catalyses Aβ42 aggregation through a heterogeneous nucleation pathway in the presence of lipid membranes. Nature Chemistry, 10(6), 673-683. doi: 10.1038/s41557-018-0046-7

Gang, H., Galvagnion, C., Meisl, G., Müller, T., Pfammatter, M., Buell, A. K., Levin, A., Dobson, C. M., Mu, B., & Knowles, T. P. J. (2018). Microfluidic Diffusion Platform for Characterizing the Sizes of Lipid Vesicles and the Thermodynamics of Protein-Lipid Interactions. Analytical Chemistry, 90(5), 3284-3290. doi: 10.1021/acs.analchem.7b04989

2017

Perni, M., Galvagnion, C., Maltsev, A., Meisl, G., Müller, M. B. D., Challa, P. K., Kirkegaard, J. B., Flagmeier, P., Cohen, S. I. A., Cascella, R., Chen, S. W., Limbocker, R., Sormanni, P., Heller, G. T., Aprile, F. A., Cremades, N., Cecchi, C., Chiti, F., Nollen, E. A. A., Knowles, T. P. J., Vendruscolo, M., Bax, A., Zasloff, M., & Dobson, C. M. (2017). A natural product inhibits the initiation of α-synuclein aggregation and suppresses its toxicity. Proceedings of the National Academy of Sciences of the United States of America, 114(6), E1009-E1017. doi: 10.1073/pnas.1610586114

Galvagnion, C. (2017). The Role of Lipids Interacting with α-Synuclein in the Pathogenesis of Parkinson’s Disease. Journal of Parkinson’s Disease, 7(3), 433-450. https://doi.org/10.3233/jpd-171103

2016

Brown, J. W. P., Buell, A. K., Michaels, T. C. T., Meisl, G., Carozza, J., Flagmeier, P., Vendruscolo, M., Knowles, T. P. J., Dobson, C. M., & Galvagnion, C. (2016). β-Synuclein suppresses both the initiation and amplification steps of α-synuclein aggregation via competitive binding to surfaces. Scientific Reports, 6, 36010. doi: 10.1038/srep36010

Flagmeier, P., Meisl, G., Vendruscolo, M., Knowles, T. P. J., Dobson, C. M., Buell, A. K., & Galvagnion, C. (2016). Mutations associated with familial Parkinson’s disease alter the initiation and amplification steps of alpha-synuclein aggregation. Proceedings of the National Academy of Sciences of the United States of America, 113(37), 10328-10333. doi: 10.1073/pnas.1604646113

Galvagnion, C., Brown, J. W. P., Ouberai, M. M., Flagmeier, P., Vendruscolo, M., Buell, A. K., Sparr, E., & Dobson, C. M. (2016). Chemical properties of lipids strongly affect the kinetics of the membrane-induced aggregation of alpha-synuclein. Proceedings of the National Academy of Sciences of the United States of America, 113(26), 7065-7070. doi: 10.1073/pnas.1601964113

Chattopadhyay, A., O’Connor, C. J., Zhang, F., Galvagnion, C., Galloway, W. R. J. D., Tan, Y. S., Stokes, J. E., Rahman, T., Verma, C., Spring, D. R., & Itzhaki, L. S. (2016). Discovery of a small-molecule binder of the oncoprotein gankyrin that modulates gankyrin activity in the cell. Scientific Reports, 6. doi: 10.1038/srep23732

2015

Granata, D., Baftizadeh, F., Habchi, J., Galvagnion, C., De Simone, A., Camilloni, C., Laio, A., & Vendruscolo, M. (2015). The inverted free energy landscape of an intrinsically disordered peptide by simulations and experiments. Scientific Reports, 5. doi: 10.1038/srep15449

Galvagnion, C., Buell, A. K., Meisl, G., Michaels, T. C. T., Vendruscolo, M., Knowles, T. P. J., & Dobson, C. M. (2015). Lipid vesicles trigger alpha-synuclein aggregation by stimulating primary nucleation. Nature Chemical Biology, 11(3), 229-U101. doi: 10.1038/nchembio.1741

Galvagnion, C., & Buell, A. K. (2015). Fundamental mechanisms of amyloid fibers by the formation of α-synuclein protein in Parkinson’s disease: Quantitative Modeling. Médecine/Sciences, 31(6-7), 597-600. https://doi.org/10.1051/medsci/20153106008

2014

Levin, A., Mason, T. O., Adler-Abramovich, L., Buell, A. K., Meisl, G., Galvagnion, C., Bram, Y., Stratford, S. A., Dobson, C. M., Knowles, T. P. J., & Gazit, E. (2014). Ostwald’s rule of stages governs structural transitions and morphology of dipeptide supramolecular polymers. Nature Communications, 5. doi: 10.1038/ncomms6261

Buell, A. K., Galvagnion, C., Gaspar, R., Sparr, E., Vendruscolo, M., Knowles, T. P. J., Linse, S., & Dobson, C. M. (2014). Solution conditions determine the relative importance of nucleation and growth processes in alpha-synuclein aggregation. Proceedings of the National Academy of Sciences of the United States of America, 111(21), 7671-7676. doi: 10.1073/pnas.1315346111

Toth, G., Gardai, S. J., Zago, W., Bertoncini, C. W., Cremades, N., Roy, S. L., Tambe, M. A., Rochet, J., Galvagnion, C., Skibinski, G., Finkbeiner, S., Bova, M., Regnstrom, K., Chiou, S., Johnston, J., Callaway, K., Anderson, J. P., Jobling, M. F., Buell, A. K., Yednock, T. A., Knowles, T. P. J., Vendruscolo, M., Christodoulou, J., Dobson, C. M., Schenk, D., & McConlogue, L. (2014). Targeting the Intrinsically Disordered Structural Ensemble of alpha-Synuclein by Small Molecules as a Potential Therapeutic Strategy for Parkinson’s Disease. PLOS ONE, 9(2). https://doi.org/10.1371/journal.pone.0087133

Pinotsi, D., Buell, A. K., Galvagnion, C., Dobson, C. M., Schierle, G. S. K., & Kaminski, C. F. (2014). Direct Observation of Heterogeneous Amyloid Fibril Growth Kinetics via Two-Color Super-Resolution Microscopy. Nano Letters, 14(1), 339-345. https://doi.org/10.1021/nl4041093

2013

Ouberai, M. M., Wang, J., Swann, M. J., Galvagnion, C., Guilliams, T., Dobson, C. M., & Welland, M. E. (2013). alpha-Synuclein Senses Lipid Packing Defects and Induces Lateral Expansion of Lipids Leading to Membrane Remodeling. July 19, 2013. https://doi.org/10.1074/jbc.M113.478297

Galvagnion, C., Montaville, P., Coic, Y. -. & Jamin, N. (2013). Production and initial structural characterization of the TM4TM5 helix-loop-helix domain of the translocator protein. Journal of Peptide Science, 19(2), 102-109. https://doi.org/10.1002/psc.2468

2009

Galvagnion, C., Smith, M. T. J., Broom, A., Vassall, K. A., Meglei, G., Gaspar, J. A., Stathopulos, P. B., Cheyne, B., & Meiering, E. M. (2009). Folding and Association of Thermophilic Dimeric and Trimeric DsrEFH Proteins: Tm0979 and Mth1491. Biochemistry, 48(13), 2891-2906. https://doi.org/10.1021/bi801784d