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Centre for Misfolding Diseases

Professor Michele Vendruscolo


In the last 15 years our research has been focused on the development of methods of characterising the structure, dynamics and interactions of proteins in previously inaccessible states. These methods are based on the use of experimental data, in particular from nuclear magnetic resonance spectroscopy, as structural restraints in molecular dynamics simulations. Through this approach it is possible to obtain information about a variety of protein conformations, as for example those populated during the folding process, and about protein interactions in complex environments, including those generating aggregate species that are associated with neurodegenerative disorders such as Alzheimer's and Parkinson's diseases.

More recently, these studies have led us to investigate the physico-chemical principles of proteins homeostasis and their application to the development of therapeutic strategies against neurodegenerative diseases. Starting from the observation that proteins are expressed in the cell at levels close to their solubility limits, we are developing approaches to prevent or delay misfolding disorders based on the enhancement of our quality control mechanisms against protein aggregation.




Chemical Kinetics for Bridging Molecular Mechanisms and Macroscopic Measurements of Amyloid Fibril Formation.
TCT Michaels, A Šarić, J Habchi, S Chia, G Meisl, M Vendruscolo, CM Dobson, TPJ Knowles
– Annu Rev Phys Chem
TEMPORARY REMOVAL: Massively parallel C. elegans tracking provides multi-dimensional fingerprints for phenotypic discovery.
M Perni, PK Challa, JB Kirkegaard, R Limbocker, M Koopman, MC Hardenberg, P Sormanni, T Müller, KL Saar, LWY Roode, J Habchi, G Vecchi, NW Fernando, S Casford, EAA Nollen, M Vendruscolo, CM Dobson, TPJ Knowles
– J Neurosci Methods
Structural basis of membrane disruption and cellular toxicity by alpha-synuclein oligomers
G Fusco, SW Chen, PTF Williamson, R Cascella, M Perni, JA Jarvis, C Cecchi, M Vendruscolo, F Chiti, N Cremades, L Ying, CM Dobson, A De Simone
– Science
Oxetane Grafts Installed Site-Selectively on Native Disulfides to Enhance Protein Stability and Activity In Vivo.
N Martínez-Sáez, S Sun, D Oldrini, P Sormanni, O Boutureira, F Carboni, I Compañón, MJ Deery, M Vendruscolo, F Corzana, R Adamo, GJL Bernardes
– Angew Chem Int Ed Engl
MobiDB 3.0: More annotations for intrinsic disorder, conformational diversity and interactions in proteins
D Piovesan, F Tabaro, L Paladin, M Necci, I Micetic, C Camilloni, N Davey, Z Dosztányi, B Mészáros, AM Monzon, G Parisi, E Schad, P Sormanni, P Tompa, M Vendruscolo, WF Vranken, SCE Tosatto
– Nucleic acids research
Delivery of Native Proteins into C. elegans Using a Transduction Protocol Based on Lipid Vesicles
M Perni, FA Aprile, S Casford, B Mannini, P Sormanni, CM Dobson, M Vendruscolo
– Scientific reports
Sequence Specificity in the Entropy-Driven Binding of a Small Molecule and a Disordered Peptide
GT Heller, FA Aprile, M Bonomi, C Camilloni, A De Simone, M Vendruscolo
– Journal of Molecular Biology
Methods of probing the interactions between small molecules and disordered proteins.
GT Heller, FA Aprile, M Vendruscolo
– Cellular and Molecular Life Sciences
The molecular chaperones DNAJB6 and Hsp70 cooperate to suppress alpha-synuclein aggregation
FA Aprile, E Källstig, G Limorenko, M Vendruscolo, D Ron, C Hansen
– Scientific reports
Rapid and accurate in silico solubility screening of a monoclonal antibody library.
P Sormanni, L Amery, S Ekizoglou, M Vendruscolo, B Popovic
– Scientific reports
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Research Interest Groups

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01223 763873

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