Dr Celine Galvagnion

Celine Galvagnion

University position

Research Associate

Departments

Department of Chemistry

Research Theme

Cellular and Molecular Neuroscience

Interests

My main research interests focus on understanding the early onset and proliferation of Parkinson’s disease.

In fact, alpha synuclein (α-syn) is a small presynaptic protein involved in neuronal and synaptic vesicle plasticity but its aggregation to form amyloid fibrils is the hallmark of Parkinson’s disease. My current research focuses on establishing the molecular mechanism by which the interaction between α-syn and vesicles trigger amyloid formation by the former. In addition, I am particularly interested in understanding how a change in bilayer properties would affect the behavior of the protein at the membrane interface. Such an understanding would allow us to shed light on the mechanism by which the balance between functional interactions of α-syn with lipid membranes and deleterious ones that can generate pathogenicity, can be affected in vivo.

Research Focus

Keywords

alpha synuclein

biophysics

amyloid

protein-lipid interaction

bilayer fluidity

Clinical conditions

Parkinson's disease

Equipment

Atomic Force Microscopy

Circular Dichroism

Fluorescence spectroscopy

Nuclear Magnetic Resonance spectroscopy

Protein purification

Recombinant protein expression

Collaborators

Cambridge

Alexander Buell

Christopher Dobson

Clemens Kaminski

Gabriele Kaminski-Schierle

Tuomas Knowles

Myriam Ouberai

Dorothea Pinotsi

Michele Vendruscolo

United Kingdom

John Christodoulou Web: http://jcgroup.biochem.ucl.ac.uk/people/...

International

Sara Linse Web: http://www.cmps.lu.se/biostru...

Emma Sparr Web: http://www.physchem.lu.se/people/...

Associated News Items


Publications

2015

Galvagnion C, Buell AK, Meisl G, Michaels TC, Vendruscolo M, Knowles TP, Dobson CM (2015), “Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation.” Nat Chem Biol Details

2014

Buell AK, Galvagnion C, Gaspar R, Sparr E, Vendruscolo M, Knowles TP, Linse S, Dobson CM (2014), “Solution conditions determine the relative importance of nucleation and growth processes in α-synuclein aggregation.” Proc Natl Acad Sci U S A Details

Levin A, Mason TO, Adler-Abramovich L, Buell AK, Meisl G, Galvagnion C, Bram Y, Stratford SA, Dobson CM, Knowles TP, Gazit E (2014), “Ostwald's rule of stages governs structural transitions and morphology of dipeptide supramolecular polymers.” Nat Commun 5:5219 Details

Pinotsi D, Buell AK, Galvagnion C, Dobson CM, Kaminski Schierle GS, Kaminski CF (2014), “Direct observation of heterogeneous amyloid fibril growth kinetics via two-color super-resolution microscopy.” Nano Lett 14(1):339-45 Details

Tóth G, Gardai SJ, Zago W, Bertoncini CW, Cremades N, Roy SL, Tambe MA, Rochet JC, Galvagnion C, Skibinski G, Finkbeiner S, Bova M, Regnstrom K, Chiou SS, Johnston J, Callaway K, Anderson JP, Jobling MF, Buell AK, Yednock TA, Knowles TP, Vendruscolo M, Christodoulou J, Dobson CM, Schenk D, McConlogue L (2014), “Targeting the Intrinsically Disordered Structural Ensemble of α-Synuclein by Small Molecules as a Potential Therapeutic Strategy for Parkinson's Disease.” PLoS One 9(2):e87133 Details

2013

Galvagnion C, Montaville P, Coïc YM, Jamin N (2013), “Production and initial structural characterization of the TM4TM5 helix-loop-helix domain of the translocator protein.” J Pept Sci 19(2):102-9 Details

Ouberai MM, Wang J, Swann MJ, Galvagnion C, Guilliams T, Dobson CM, Welland ME (2013), “α-Synuclein senses lipid packing defects and induces lateral expansion of lipids leading to membrane remodeling.” J Biol Chem 288(29):20883-95 Details

2009

Galvagnion C, Smith MT, Broom A, Vassall KA, Meglei G, Gaspar JA, Stathopulos PB, Cheyne B, Meiering EM (2009), “Folding and association of thermophilic dimeric and trimeric DsrEFH proteins: Tm0979 and Mth1491.” Biochemistry 48(13):2891-906 Details

2008

Rumfeldt JA, Galvagnion C, Vassall KA, Meiering EM (2008), “Conformational stability and folding mechanisms of dimeric proteins.” Prog Biophys Mol Biol 98(1):61-84 Details