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Centre for Misfolding Diseases

Professor of Biophysics

Our research

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.

Application to neurodegenerative 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.

Watch Professor Vendruscolo discuss his research

Take a tour of the Una Finlay Laboratory in the Centre for Misfolding Diseases

Publications

Multidimensional Protein Solubility Optimization with an Ultrahigh-Throughput Microfluidic Platform.
NA Erkamp, M Oeller, T Sneideris, H Ausserwoger, A Levin, TJ Welsh, R Qi, D Qian, N Lorenzen, H Zhu, P Sormanni, M Vendruscolo, TPJ Knowles
– Analytical chemistry
(2023)
95,
5362
Sequence-based prediction of the solubility of peptides containing non-natural amino acids
M Oeller, R Kang, H Bolt, A Gomes dos Santos, A Langborg Weinmann, A Nikitidis, P Zlatoidsky, W Su, W Czechtizky, L De Maria, P Sormanni, M Vendruscolo
(2023)
Extracellular protein homeostasis in neurodegenerative diseases.
MR Wilson, S Satapathy, M Vendruscolo
– Nature Reviews Neurology
(2023)
19,
235
Spontaneous nucleation and fast aggregate-dependent proliferation of α-synuclein aggregates within liquid condensates at neutral pH.
ST Dada, MC Hardenberg, Z Toprakcioglu, LK Mrugalla, MP Cali, MO McKeon, E Klimont, TCT Michaels, TPJ Knowles, M Vendruscolo
– Proceedings of the National Academy of Sciences of USA
(2023)
120,
e2208792120
Amyloidogenic proteins in the SARS-CoV and SARS-CoV-2 proteomes.
T Bhardwaj, K Gadhave, SK Kapuganti, P Kumar, ZF Brotzakis, KU Saumya, N Nayak, A Kumar, R Joshi, B Mukherjee, A Bhardwaj, KG Thakur, N Garg, M Vendruscolo, R Giri
– Nature communications
(2023)
14,
945
Varied mechanisms for the neutralization of biological toxins using natural products
R Limbocker, J Gabriel, T Tan, DJ Rinauro, M Vendruscolo
– Biophysical journal
(2023)
122,
21a
Combinations of Vitamin A and Vitamin E Metabolites Confer Resilience against Amyloid-β Aggregation
P Joshi, S Chia, X Yang, M Perni, JM Gabriel, M Gilmer, R Limbocker, J Habchi, M Vendruscolo
– ACS Chemical Neuroscience
(2023)
14,
657
Sequence-based prediction of pH-dependent protein solubility using CamSol
M Oeller, R Kang, R Bell, H Ausserwöger, P Sormanni, M Vendruscolo
– Briefings in Bioinformatics
(2023)
24,
bbad004
AlphaFold Prediction of Structural Ensembles of Disordered Proteins
F Brotzakis, S Zhang, M Vendruscolo
(2023)
Enhanced surface nanoanalytics of transient biomolecular processes
AM Miller, S Chia, Z Toprakcioglo, T Hakala, R Schmid, Y Feng, T Kartanas, A Kamada, M Vendruscolo, FS Ruggeri, T Knowles
– Science Advances
(2023)
9,
eabq3151
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Co-Director

Research Interest Groups

Telephone number

01223 763873

Email address