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Researcher profile

Tuomas P. J. Knowles

Tuomas P. J. Knowles contributes to research discovery and scholarly infrastructure.

ResearcherAffiliation not importedOpen to collaborate
Biological PhysicsBiomoleculescond-mat.softMolecular Networks

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Published work

2 published item(s)

preprint2026arXiv

Tracer-free Contactless Acoustic Microrheometry Quantifies Viscoelastic Spectrum of Phase-separated Condensates

The rheology of phase-separated condensates plays a central role in applications spanning advanced materials design and cellular processes, yet quantitative characterization of their viscoelasticity remains challenging due to the limitations of existing microrheological methods that require tracer particles or mechanical contact. Here, we establish tracer-free and contactless acoustic microrheometry as a versatile platform for quantifying the frequency-dependent complex shear modulus of single microscale condensates over 0.01-10 Hz. Using spatiotemporally controlled acoustic radiation force generated within a micro-acoustic resonator, this method deforms condensates for creep-recovery and oscillatory viscoelastic measurements. Quantitative validation using dextran condensates in a polyethylene-glycol continuous phase successfully captures their size- and frequency-dependent mechanical responses, while application to nucleic-acid condensates reveals salt-dependent internal viscoelastic changes at single-condensate resolution. By enabling quantitative dissection of condensate mechanics without invasive probes, acoustic microrheometry provides a broadly applicable framework for investigating phase-separated condensates across materials science, soft matter physics, biology, and beyond.

0 citations0 reviewsNo code linkedOpen access
preprint2016arXiv

A general reaction network unifies the aggregation behaviour of the A$β$42 peptide and its variants

The amyloid $β$ peptide (A$β$42), whose aggregation is associated with Alzheimer's disease, is an amphiphatic peptide with a high propensity to self-assemble. A$β$42 has a net negative charge at physiological pH and modulations of intermolecular electrostatic interactions can significantly alter its aggregation behaviour. Variations in sequence and solution conditions lead to varied macroscopic behaviour, often resulting in a number of different mechanistic explanations for the aggregation of these closely related systems. Here we alter the electrostatic interactions governing the fibril aggregation kinetics by varying the ionic strength over an order of magnitude, which allows us to sample the space of different reaction mechanisms, and develop a minimal reaction network that explains the experimental kinetics under all the different conditions. We find that an increase in the ionic strength leads to an increased rate of surface catalysed nucleation over fragmentation and eventually to a saturation of this nucleation process. More generally, this reaction network connects previously separate systems, such as mutants of A$β$42 and the wild type, on a continuous mechanistic landscape, thereby providing a unified picture of the aggregation mechanism of A$β$42 and the means of directly comparing the effects of intrinsic modifications of the peptide to those of simple electrostatic shielding.

0 citations0 reviewsNo code linkedOpen access