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Department of Chemistry

Portrait of tpjk2

We study the physical and chemical aspects of the behaviour of biopolymers and other soft systems. Much of our work has been focused on the physical aspects underlying the self-assembly of protein molecules. Self-organisation is the driving force generating complex matter in nature, and the process by which the machinery providing functionality in living systems is assembled. The goal of our research is to understand the physical and chemical factors which control the structures and dynamics of biomolecular assemblies, and the connections between the nanoscale characteristics of the component molecules and the physical properties of large-scale assemblies and their behaviour on a mesoscopic to macroscopic scale. The techniques used in our laboratory include biosensors, optical lithography, microfluidic devices and scanning probe microscopy and spectroscopy. We work both with natural and synthetic polymers and our interests range from fundamental chemical physics to technological applications in material science and molecular medicine.


Single molecule secondary structure determination of proteins through infrared absorption nanospectroscopy
FS Ruggeri, B Mannini, R Schmid, M Vendruscolo, TPJ Knowles
– Nature Communications
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
– Nature nanotechnology
Thermodynamic and kinetic design principles for amyloid-aggregation inhibitors
TCT Michaels, A Šarić, G Meisl, GT Heller, S Curk, P Arosio, S Linse, CM Dobson, M Vendruscolo, TPJ Knowles
– Proc Natl Acad Sci U S A
Phase Transition and Crystallization Kinetics of a Supramolecular System in a Microfluidic Platform
D Cohen-Gerassi, ZA Arnon, T Guterman, A Levin, M Ghosh, M Aviv, D Levy, TPJ Knowles, Y Shacham-Diamand, L Adler-Abramovich
– Chemistry of Materials
Amelioration of aggregate cytotoxicity by catalytic conversion of protein oligomers into amyloid fibrils.
J Yang, AJ Dear, Q-Q Yao, Z Liu, CM Dobson, TPJ Knowles, S Wu, S Perrett
– Nanoscale
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
Kinetic analysis reveals the rates and mechanisms of protein aggregation in a multicellular organism
T Sinnige, G Meisl, T Michaels, M Vendruscolo, TPJ Knowles, R Morimoto
Direct measurement of lipid membrane disruption connects kinetics and toxicity of Aβ42 aggregation.
P Flagmeier, S De, TCT Michaels, X Yang, AJ Dear, C Emanuelsson, M Vendruscolo, S Linse, D Klenerman, TPJ Knowles, CM Dobson
– Nature structural & molecular biology
Multidimensional protein characterisation using microfluidic post-column analysis
T Scheidt, T Kartanas, Q Peter, MM Schneider, KL Saar, T Müller, PK Challa, A Levin, S Devenish, TPJ Knowles
– Lab Chip
A microfluidic strategy for the detection of membrane protein interactions
Y Zhang, TW Herling, S Kreida, QAE Peter, T Kartanas, S Törnroth-Horsefield, S Linse, TPJ Knowles
– Lab Chip
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01223 336344

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