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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.

Publications

Trodusquemine enhances A beta(42) aggregation but suppresses its toxicity by displacing oligomers from cell membranes
R Limbocker, S Chia, FS Ruggeri, M Perni, R Cascella, GT Heller, G Meisl, B Mannini, J Habchi, TCT Michaels, PK Challa, M Ahn, ST Casford, N Fernando, CK Xu, ND Kloss, SIA Cohen, JR Kumita, C Cecchi, M Zasloff, S Linse, TPJ Knowles, F Chiti, M Vendruscolo, CM Dobson
– Nature Communications
(2019)
10,
225
Universality of filamentous aggregation phenomena
TCT Michaels, AJ Dear, TPJ Knowles
– Physical Review E
(2019)
99,
062415
Analysis of αB-crystallin polydispersity in solution through native microfluidic electrophoresis
MA Wright, FS Ruggeri, KL Saar, PK Challa, JLP Benesch, TPJ Knowles
– Analyst
(2019)
144,
4413
Programmable On-Chip Artificial Cell Producing Post-Translationally Modified Ubiquitinated Protein
S Zilberzwige-Tal, A Levin, Z Toprakcioglu, TPJ Knowles, E Gazit, J Elbaz
– Small
(2019)
e1901780
Different soluble aggregates of Aβ42 can give rise to cellular toxicity through different mechanisms
S De, DC Wirthensohn, P Flagmeier, C Hughes, FA Aprile, FS Ruggeri, DR Whiten, D Emin, Z Xia, JA Varela, P Sormanni, F Kundel, TPJ Knowles, CM Dobson, C Bryant, M Vendruscolo, D Klenerman
– Nat Commun
(2019)
10,
1541
The Amyloid Phenomenon and Its Significance in Biology and Medicine
CM Dobson, TPJ Knowles, M Vendruscolo
– Cold Spring Harbor perspectives in biology
(2019)
a033878
Secondary nucleation and elongation occur at different sites on Alzheimer's amyloid-beta aggregates
T Scheidt, U Łapińska, JR Kumita, DR Whiten, D Klenerman, MR Wilson, SIA Cohen, S Linse, M Vendruscolo, CM Dobson, TPJ Knowles, P Arosio
– Science Advances
(2019)
5,
eaau3112
Direct observation of prion protein oligomer formation reveals an aggregation mechanism with multiple conformationally distinct species.
JC Sang, J-E Lee, AJ Dear, S De, G Meisl, AM Thackray, R Bujdoso, TPJ Knowles, D Klenerman
– Chem Sci
(2019)
10,
4588
Quaternization of Vinyl/Alkynyl Pyridine Enables Ultrafast Cysteine-Selective Protein Modification and Charge Modulation
MJ Matos, CD Navo, T Hakala, X Ferhati, A Guerreiro, D Hartmann, B Bernardim, KL Saar, I Compañón, F Corzana, TPJ Knowles, G Jiménez-Osés, GJL Bernardes
– Angewandte Chemie - International Edition
(2019)
58,
6640
A method of predicting the in vitro fibril formation propensity of Aβ40 mutants based on their inclusion body levels in E. coli
K Sanagavarapu, E Nüske, I Nasir, G Meisl, JN Immink, P Sormanni, M Vendruscolo, TPJ Knowles, A Malmendal, C Cabaleiro-Lago, S Linse
– Scientific Reports
(2019)
9,
3680
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Research Interest Groups

Telephone number

01223 336344

Email address

tpjk2@cam.ac.uk