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Department of Chemistry

Portrait of mv245


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.




Single molecule secondary structure determination of proteins through infrared absorption nanospectroscopy
FS Ruggeri, B Mannini, R Schmid, M Vendruscolo, TPJ Knowles
– Nat Commun
Rationally designed antibodies as research tools to study the > structure-toxicity relationship of amyloid-b oligomers
R Limbocker, B Mannini, R Cataldi, S Chhangur, AK Wright, RP Kreiser, JA Albright, S Chia, J Habchi, P Sormanni, JR Kumita, FS Ruggeri, CM Dobson, F Chiti, FA Aprile, M Vendruscolo
– International journal of molecular sciences
Rational design of a conformation-specific antibody for the quantification of Aβ oligomers
FA Aprile, P Sormanni, M Podpolny, S Chhangur, L-M Needham, FS Ruggeri, M Perni, R Limbocker, GT Heller, T Sneideris, T Scheidt, B Mannini, J Habchi, SF Lee, PC Salinas, TPJ Knowles, CM Dobson, M Vendruscolo
– Proceedings of the National Academy of Sciences
Reduced proteasome activity in the aging brain results in ribosome stoichiometry loss and aggregation.
E Kelmer Sacramento, JM Kirkpatrick, M Mazzetto, M Baumgart, A Bartolome, S Di Sanzo, C Caterino, M Sanguanini, N Papaevgeniou, M Lefaki, D Childs, S Bagnoli, E Terzibasi Tozzini, D Di Fraia, N Romanov, PH Sudmant, W Huber, N Chondrogianni, M Vendruscolo, A Cellerino, A Ori
– Molecular Systems Biology
Sequence-based prediction of protein binding mode landscapes
A Horvath, M Miskei, V Ambrus, M Vendruscolo, M Fuxreiter
– PLOS Computational Biology
Assessing motor-related phenotypes of Caenorhabditis elegans with the wide field-of-view nematode tracking platform
M Koopman, Q Peter, RI Seinstra, M Perni, M Vendruscolo, CM Dobson, TPJ Knowles, EAA Nollen
– Nature protocols
Complexity in Lipid Membrane Composition Induces Resilience to A beta(42) Aggregation
M Sanguanini, KN Baumann, S Preet, S Chia, J Habchi, TPJ Knowles, M Vendruscolo
– ACS Chem Neurosci
Dynamics of oligomer populations formed during the aggregation of Alzheimer’s Aβ42 peptide
TCT Michaels, A Šarić, S Curk, K Bernfur, P Arosio, G Meisl, AJ Dear, SIA Cohen, CM Dobson, M Vendruscolo, S Linse, TPJ Knowles
– Nat Chem
Author Correction: Dynamics of oligomer populations formed during the aggregation of Alzheimer's Aβ42 peptide.
TCT Michaels, A Šarić, S Curk, K Bernfur, P Arosio, G Meisl, AJ Dear, SIA Cohen, CM Dobson, M Vendruscolo, S Linse, TPJ Knowles
– Nat Chem
A Cell- and Tissue-Specific Weakness of the Protein Homeostasis System Underlies Brain Vulnerability to Protein Aggregation
R Kundra, CM Dobson, M Vendruscolo
– iScience
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