Professor Michele Vendruscolo

Michele Vendruscolo

University position


Professor Michele Vendruscolo is pleased to consider applications from prospective PhD students.


Department of Chemistry


Centre for Misfolding Diseases


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Research Themes

Systems and Computational Neuroscience

Cellular and Molecular Neuroscience


Our research at the Centre for Misfolding Diseases ( is aimed at understanding the molecular origins of neurodegenerative disorders.

We have set up an interdisciplinary programme that brings together methods and concepts from chemistry, physics, engineering, genetics and medicine. We are using a combination of in vitro, in silico and in vivo approaches to study protein homeostasis through the analysis of the effects that result from its alteration in specific proteins, from either amino acid mutations, or changes in concentration and solubility, or the interactions with other molecules.

This programme is generating new insights into the mechanism through which physical and chemical sciences can increase our understanding of the nature and consequences of the failure to maintain protein homeostasis and its association with ageing and neurodegenerative disorders.

Widespread aggregation and neurodegenerative diseases are associated with supersaturated proteins.
Widespread aggregation and neurodegenerative diseases are associated with supersaturated proteins.
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Research Focus



protein aggregation

biophysical methods

Clinical conditions

Alzheimer's disease

Parkinson's disease


Cell culture

Computational modelling

Confocal microscopy

Fluorescence microscopy



Protein purification

Recombinant protein expression



Mario De Bono

Christopher Dobson

Clemens Kaminski

Tuomas Knowles

Peter St George-Hyslop


Fabrizio Chiti Web:

Sara Linse Web:

Rick Morimoto Web:

Ellen Nollen Web:

Associated News Items

Key publications

Cohen SI, Arosio P, Presto J, Kurudenkandy FR, Biverstål H, Dolfe L, Dunning C, Yang X, Frohm B, Vendruscolo M, Johansson J, Dobson CM, Fisahn A, Knowles TP, Linse S. (2015), “A molecular chaperone breaks the catalytic cycle that generates toxic A? oligomers” Nat. Struct. Mol. Biol. 22(3): 207-213

Murakami T, Qamar S, Lin JQ, Schierle GS, Rees E, Miyashita A, Costa AR, Dodd RB, Chan FT, Michel CH, Kronenberg-Versteeg D, Li Y, Yang SP, Wakutani Y, Meadows W, Ferry RR, Dong L, Tartaglia GG, Favrin G, Lin WL, Dickson DW, Zhen M, Ron D, Schmitt-Ulms G, Fraser PE, Shneider NA, Holt C, Vendruscolo M, Kaminski CF, St George-Hyslop P. (2015), “ALS/FTD Mutation-Induced Phase Transition of FUS Liquid Droplets and Reversible Hydrogels into Irreversible Hydrogels Impairs RNP Granule Function.” Neuron Nov 18;88(4): 678-690

Ciryam P, Tartaglia GG, Morimoto RI, Dobson CM, Vendruscolo M (2013), “Widespread aggregation and neurodegenerative diseases are associated with supersaturated proteins.” Cell Rep 5(3):781-90 Details

Tartaglia GG, Pawar AP, Campioni S, Dobson CM, Chiti F, Vendruscolo M (2008), “Prediction of aggregation-prone regions in structured proteins.” J Mol Biol 380(2):425-36 Details

Tartaglia GG, Pechmann S, Dobson CM and Vendruscolo M (2007), “Life on the Edge: A link between gene expression levels and aggregation rates of human proteins” Trends Biochem Sci 32:204-206 Details



Galvagnion C, Buell AK, Meisl G, Michaels TC, Vendruscolo M, Knowles TP, Dobson CM. (2015), “Lipid vesicles trigger ?-synuclein aggregation by stimulating primary nucleation” Nat. Chem. Biol. 11(3): 229-234


Arosio P, Vendruscolo M, Dobson CM, Knowles TP (2014), “Chemical kinetics for drug discovery to combat protein aggregation diseases.” Trends Pharmacol Sci 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 ?-Synuclein by Small Molecules as a Potential Therapeutic Strategy for Parkinson's Disease.” PLoS One 9(2):e87133 Details


Cohen SI, Linse S, Luheshi LM, Hellstrand E, White DA, Rajah L, Otzen DE, Vendruscolo M, Dobson CM, Knowles TP (2013), “Proliferation of amyloid-?42 aggregates occurs through a secondary nucleation mechanism.” Proc Natl Acad Sci U S A 110(24):9758-63 Details

Fitzpatrick AW, Debelouchina GT, Bayro MJ, Clare DK, Caporini MA, Bajaj VS, Jaroniec CP, Wang L, Ladizhansky V, Müller SA, MacPhee CE, Waudby CA, Mott HR, De Simone A, Knowles TP, Saibil HR, Vendruscolo M, Orlova EV, Griffin RG, Dobson CM (2013), “Atomic structure and hierarchical assembly of a cross-? amyloid fibril.” Proc Natl Acad Sci U S A 110(14):5468-73 Details


Neudecker P, Robustelli P, Cavalli A, Walsh P, Lundström P, Zarrine-Afsar A, Sharpe S, Vendruscolo M, Kay LE (2012), “Structure of an intermediate state in protein folding and aggregation.” Science 336(6079):362-6 Details

Vendruscolo M (2012), “Proteome folding and aggregation.” Curr Opin Struct Biol 22(2):138-43 Details


Baldwin AJ, Knowles TP, Tartaglia GG, Fitzpatrick AW, Devlin GL, Shammas SL, Waudby CA, Mossuto MF, Meehan S, Gras SL, Christodoulou J, Anthony-Cahill SJ, Barker PD, Vendruscolo M, Dobson CM (2011), “Metastability of native proteins and the phenomenon of amyloid formation.” J Am Chem Soc 133(36):14160-3 Details

Olzscha H, Schermann SM, Woerner AC, Pinkert S, Hecht MH, Tartaglia GG, Vendruscolo M, Hayer-Hartl M, Hartl FU, Vabulas RM (2011), “Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions.” Cell 144(1):67-78 Details