Educational background

I completed my BSc in Biochemistry at the Lebanese University during which I became interested in understanding the protein folding process. In order to pursue my interests, I joined an MSc programme in Aix-Marseille University, France, where I studied the folding of unstructured proteins, namely intrinsically disordered proteins.

My research during my MSc and PhD was centred on understanding the molecular mechanisms by which the folding of disordered proteins upon binding to their partners results in the gain of a function, which leads in some cases to human diseases. In particular, I studied the role of intrinsically disordered proteins in orchestrating the replicative machinery of RNA virsues.

Current research

After my PhD, I joined the Centre for Misfolding Diseases, where my research to date mainly focuses on the generation of new methods that allow the detailed understanding of the molecular principles underlying the misfolding of intrinsically disordered proteins, a hallmark of many diseases, such as Alzheimer’s and Parkinson’s diseases, for the aim of drug discovery.

At the Centre, I have worked on elucidating the fundamental principles of protein aggregation and on developing quantitative tools for the assessment of the efficacy of drug molecules in modulating the protein aggregation process. In collaboration with many colleagues and based on the accumulated knowledge in the Centre, we have set up an innovative and interdisciplinary drug discovery programme that aims at the selective targeting of specific microscopic processes in a controlled intervention during the aggregation of proteins associated with misfolding diseases, in particular Alzheimer’s and Parkinson’s diseases. A direct consequence of this endeavour was the ability to reach, for the first time, a detailed understanding of the mode of action of drug molecules on single microscopic steps during the aggregation process.

Research translation

This contribution has led to the translation of the drug discovery programme into practice by creating Wren Therapeutics, a biopharmaceutical company, in which I am currently the Head of R&D. Wren Therapeutics aims at bridging the gap between fundamental and translational research in order to generate transformative treatments across a wide range of protein misfolding diseases.

Publications

Dynamics of the Intrinsically Disordered C-Terminal Domain of the Nipah Virus Nucleoprotein and Interaction with the X Domain of the Phosphoprotein as Unveiled by NMR Spectroscopy
L Baronti, J Erales, J Habchi, IC Felli, R Pierattelli, S Longhi
Chembiochem
(2014)
16
Extracting structural information from charge-state distributions of intrinsically disordered proteins by non-denaturing electrospray-ionization mass spectrometry
L Testa, S Brocca, C Santambrogio, A D'Urzo, J Habchi, S Longhi, VN Uversky, R Grandori
Intrinsically Disordered Proteins
(2014)
1
Impact of crystal packing on coiled-coil flexibility.
F Ferron, D Blocquel, J Habchi, E Durand, M Sevajol, J Erales, N Papageorgiou, S Longhi
Acta Crystallographica Section A: Foundations and advances
(2014)
70
Coiled-coil deformations in crystal structures: themeasles virusphosphoprotein multimerization domain as an illustrative example
D Blocquel, J Habchi, E Durand, M Sevajol, F Ferron, J Erales, N Papageorgiou, S Longhi
Acta Crystallographica Section D, Structural Biology
(2014)
70
Structural Disorder in Viral Proteins
B Xue, D Blocquel, J Habchi, AV Uversky, L Kurgan, VN Uversky, S Longhi
Chem Rev
(2014)
114
Introducing protein intrinsic disorder
J Habchi, P Tompa, S Longhi, VN Uversky
Chemical reviews
(2014)
114
Diversification of EPR signatures in Site Directed Spin Labeling using a β-phosphorylated nitroxide.
N Le Breton, M Martinho, K Kabytaev, J Topin, E Mileo, D Blocquel, J Habchi, S Longhi, A Rockenbauer, J Golebiowski, B Guigliarelli, SRA Marque, V Belle
Physical Chemistry Chemical Physics
(2014)
16
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
Coiled-coil deformations in crystal structures: The measles virus phosphoprotein multimerization domain as an illustrative example
D Blocquel, J Habchi, E Durand, M Sevajol, F Ferron, J Erales, N Papageorgiou, S Longhi
Acta Crystallographica Section D Biological Crystallography
(2014)
70
Atomic resolution description of the interaction between the nucleoprotein and phosphoprotein of Hendra virus.
G Communie, J Habchi, F Yabukarski, D Blocquel, R Schneider, N Tarbouriech, N Papageorgiou, RWH Ruigrok, M Jamin, MR Jensen, S Longhi, M Blackledge
PLoS Pathogens
(2013)
9

Research Staff Scientist

Telephone number

01223 336427 (shared)

Email address