skip to content

Centre for Misfolding Diseases

Dr Johnny Habchi

I am interested in studying a particular family of proteins, namely intrinsically disordered proteins (IDPs). IDPs are proteins that lack a well-defined 3D structure under physiological conditions and in the absence of a partner. These proteins are currently receiving much attention from the Protein Science community, as they are crucial for many cell functions. Indeed, due to the lack of a precise structure, IDPs are characterized by a high flexibility that allows them interacting with multiple partners and hence exerting multiple biological functions. In order to be functional, in most of the cases specific regions within IDPs undergo an induced folding that is triggered by either binding to their biological partner or environmental changes. On the other hand, under pathological conditions they could undertake an alternative pathway and aggregate into amyloid fibrils. These latter constitute the hallmark of many debilitating diseases such as Alzheimer, Parkinson and diabetes, to name few. During my Masters, PhD and Postdoc, using a wide range of biochemical and biophysical tools, I studied both pathways that IDPs can undertake (i.e. folding upon binding to their partners and aggregation into amyloid fibrils) for the aim of drug design.

I am currently working on Amyloid-beta, a small IDP, which constitutes the main component in brain deposits (i.e. protein aggregates) that constitutes a hallmark of Alzheimer’s disease. The aim of my post-doctoral project is to develop a novel strategy that could lead to the identification of efficient drug candidates against Amyloid-beta aggregation. 


AFM-Based Single Molecule Techniques: Unraveling the Amyloid Pathogenic Species.
FS Ruggeri, J Habchi, A Cerreta, G Dietler
– Current Pharmaceutical Design
A Fragment-Based Method of Creating Small-Molecule Libraries to Target the Aggregation of Intrinsically Disordered Proteins
P Joshi, S Chia, J Habchi, TPJ Knowles, CM Dobson, M Vendruscolo
– ACS Comb Sci
Neuroscience: An anticancer drug suppresses the primary nucleation reaction that initiates the production of the toxic Ab42 aggregates linked with Alzheimer's disease
J Habchi, P Arosio, M Perni, AR Costa, M Yagi-Utsumi, P Joshi, S Chia, SIA Cohen, MBD Müller, S Linse, EAA Nollen, CM Dobson, TPJ Knowles, M Vendruscolo
– Sci Adv
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
Neuronal Cx3cr1 Deficiency Protects against Amyloid β-Induced Neurotoxicity.
J Dworzak, B Renvoisé, J Habchi, EV Yates, C Combadière, TP Knowles, CM Dobson, C Blackstone, O Paulsen, PM Murphy
– PLoS One
Structural disorder within paramyxoviral nucleoproteins and phosphoproteins in their free and bound forms: From predictions to experimental assessment
J Habchi, S Longhi
– International journal of molecular sciences
Order and Disorder in the Replicative Complex of Paramyxoviruses.
J Erales, D Blocquel, J Habchi, M Beltrandi, A Gruet, M Dosnon, C Bignon, S Longhi
– Advances in experimental medicine and biology
The inverted free energy landscape of an intrinsically disordered peptide by simulations and experiments.
D Granata, F Baftizadeh, J Habchi, C Galvagnion, A De Simone, C Camilloni, A Laio, M Vendruscolo
– Scientific reports
Molecular basis for structural heterogeneity of an intrinsically disordered protein bound to a partner by combined ESI-IM-MS and modeling
A D'Urzo, A Konijnenberg, G Rossetti, J Habchi, J Li, P Carloni, F Sobott, S Longhi, R Grandori
– Journal of The American Society for Mass Spectrometry
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
  • 1 of 3
  • >

Research Staff Scientists

Telephone number

01223 336427 (shared)

Email address