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Yusuf Hamied Department of Chemistry

 

Professor Michele Vendruscolo

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

Conformational Equilibrium between the Sub States of the Acidic Denatured State of ACBP Determined by NMR Chemical Shifts and Metadynamics
C Camilloni, M Vendruscolo
– Biophysical Journal
(2014)
106,
459A
(doi: 10.1016/j.bpj.2013.11.2605)
MD Simulations of Intrinsically Disordered Proteins with Replica-Averaged Chemical Shift Restraints
B Fu, P Kukic, C Camilloni, M Vendruscolo
– Biophysical Journal
(2014)
106,
481A
(doi: 10.1016/j.bpj.2013.11.2714)
Determination of Primary Nucleation Mechanisms of α-Synuclein Amyloid Aggregation
FA Aprile, G Meisl, AK Buell, P Flagmeier, CM Dobson, M Vendruscolo, TPJ Knowles
– Biophysical Journal
(2014)
106,
268a
(doi: 10.1016/j.bpj.2013.11.1570)
Chemical kinetics for drug discovery to combat protein aggregation diseases
P Arosio, M Vendruscolo, CM Dobson, TPJ Knowles
– Trends in Pharmacological Sciences
(2014)
35,
127
Structural investigation of the folding of an immunoglobulin domain on the ribosome using NMR Spectroscopy
A Cassaignau, L Cabrita, C Waudby, X Wang, H Launay, C Camilloni, M-E Karyadi, S Chan, M Vendruscolo, C Dobson, J Christodoulou
– FASEB JOURNAL
(2014)
28,
(link to publication)
Structural and Mechanistic Analyses of the Effects of Small Compounds on Amyloid Beta Self-Assembly
J Habchi, P Joshi, A Spilotros, D Svergun, M Vendruscolo
– BIOPHYSICAL JOURNAL
(2014)
106,
268A
(link to publication)
A Clear View of Polymorphism, Twist, and Chirality in Amyloid Fibril Formation
LR Volpatti, M Vendruscolo, CM Dobson, TPJ Knowles
– ACS Nano
(2013)
7,
10443
(doi: 10.1021/nn406121w)
Higher Order Amyloid Fibril Structure by MAS NMR and DNP Spectroscopy
GT Debelouchina, MJ Bayro, AW Fitzpatrick, V Ladizhansky, MT Colvin, MA Caporini, CP Jaroniec, VS Bajaj, M Rosay, CE Macphee, M Vendruscolo, WE Maas, CM Dobson, RG Griffin
– J Am Chem Soc
(2013)
135,
19237
(doi: 10.1021/ja409050a)
Replica-Averaged Metadynamics
C Camilloni, A Cavalli, M Vendruscolo
– J Chem Theory Comput
(2013)
9,
5610
(doi: 10.1021/ct4006272)
Widespread aggregation and neurodegenerative diseases are associated with supersaturated proteins.
P Ciryam, GG Tartaglia, RI Morimoto, CM Dobson, M Vendruscolo
– Cell Rep
(2013)
5,
781
(doi: 10.1016/j.celrep.2013.09.043)
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Research Groups

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Telephone number

01223 763873

Email address

mv245@cam.ac.uk

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