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Centre for Misfolding Diseases

Research Associate

I currently work at the Centre for Misfolding Diseases at the University of Cambridge. The focus of my original research programme is to develop and apply new Physical methods at the interface with Chemistry and Biology to shed light on the molecular processes underlying the onset of neurodegenerative disorders and study functional biomaterials for biomedical applications.



In my research, I continuously push the boundaries of the methods of analysis of modern biology and physics for investigating complex and heterogeneous biological samples and biomaterials at the nanoscale. I have deep expertise in scanning probe microscopy, surface science, spectroscopy, data analysis, image processing and single particle characterisation.


For a complete list of publications please see below:

Publications

Infrared nanospectroscopy reveals the molecular interaction fingerprint of an aggregation inhibitor with single Aβ42 oligomers
FS Ruggeri, J Habchi, S Chia, RI Horne, M Vendruscolo, TPJ Knowles
– Nature Communications
(2021)
12,
688
Amyloid precipitation in biofluids using a structure-specific chemical antibody
M Rodrigues, P Bhattacharjee, A Brinkmalm, D Do, C Pearson, S De, A Ponjavic, J Varela, F Ruggeri, I Baudrexel, J Lee, A Carr, K Kulenkampff, T Knowles, H Zetterberg, T Snaddon, S Gandhi, S Lee, D Klenerman
(2020)
Small-molecule sequestration of amyloid-β as a drug discovery strategy for Alzheimer's disease
GT Heller, FA Aprile, TCT Michaels, R Limbocker, M Perni, FS Ruggeri, B Mannini, T Löhr, M Bonomi, C Camilloni, A De Simone, IC Felli, R Pierattelli, TPJ Knowles, CM Dobson, M Vendruscolo
– Sci Adv
(2020)
6,
eabb5924
The Hsc70 Disaggregation Machinery Removes Monomer Units Directly from α-Synuclein Fibril Ends
M Schneider, S Gautam, T Herling, E Andrzejewska, G Krainer, A Miller, Q Peter, FS Ruggeri, M Vendruscolo, A Bracher, C Dobson, U Hartl, T Knowles
(2020)
2020.11.02.365825
A rationally designed bicyclic peptide remodels Aβ42 aggregation in vitro and reduces its toxicity in a worm model of Alzheimer's disease.
T Ikenoue, FA Aprile, P Sormanni, FS Ruggeri, M Perni, GT Heller, CP Haas, C Middel, R Limbocker, B Mannini, TCT Michaels, TPJ Knowles, CM Dobson, M Vendruscolo
– Scientific Reports
(2020)
10,
15280
Biomolecular condensates undergo a generic shear-mediated liquid-to-solid transition.
Y Shen, FS Ruggeri, D Vigolo, A Kamada, S Qamar, A Levin, C Iserman, S Alberti, PS George-Hyslop, TPJ Knowles
– Nat Nanotechnol
(2020)
15,
841
Trodusquemine displaces protein misfolded oligomers from cell membranes and abrogates their cytotoxicity through a generic mechanism.
R Limbocker, B Mannini, FS Ruggeri, R Cascella, CK Xu, M Perni, S Chia, SW Chen, J Habchi, A Bigi, RP Kreiser, AK Wright, JA Albright, T Kartanas, JR Kumita, N Cremades, M Zasloff, C Cecchi, TPJ Knowles, F Chiti, M Vendruscolo, CM Dobson
– Communications Biology
(2020)
3,
435
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
(2020)
21,
E4542
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 of the United States of America
(2020)
117,
13509
Single molecule secondary structure determination of proteins through infrared absorption nanospectroscopy.
FS Ruggeri, B Mannini, R Schmid, M Vendruscolo, TPJ Knowles
– Nature communications
(2020)
11,
2945
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Postdoctoral researcher

Telephone number

01223 763842