TYC Recently Appointed Academic Talks: Carla de Tomas, King’s, Gabriella Heller, UCL & Ivan Palaia – King’s

To welcome new PIs to the TYC, and to introduce them and their research to existing members, the Thomas Young Centre runs a continuous programme of Recently Recruited events.

This session introduces Carla de Tomas, Gabriella Heller and Ivan Palaia to the TYC.

Designing next-generation carbon materials – Carla de Tomas, King’s College London
Nanoporous carbon materials play a crucial role in a range of industrial applications, including water purification, gas separation, and energy storage—particularly as electrodes in alkali-ion batteries. Their exceptional performance stems from a complex internal structure featuring a diverse distribution of pore sizes and geometries. As a result, detailed structural
characterization is essential to assess, optimize, and scale up their synthesis and functional performance.

Over the past few decades, a variety of methods have been employed to study porosity and related properties—such as surface area, pore size distribution (PSD), and real density—using gas adsorption techniques. However, these models typically rely on simplified one-dimensional representations of carbon nanopores, such as slit-pore geometries. In reality, the adsorption and separation behavior of nanoporous carbons is governed by their three-dimensional pore architecture. Advancing techniques to estimate the 3D nanostructure of these materials from gas adsorption data would significantly accelerate both fundamental research and the optimization of nanoporous carbon electrodes.

Drugging Intrinsically Disordered Proteins – Gabriella Heller, UCL & Bind Research
Intrinsically disordered proteins are highly dynamic biomolecules that rapidly interconvert among many structural conformations. These dynamic proteins are involved in cancers, neurodegeneration, cardiovascular illnesses, and viral infections. Despite their enormous therapeutic potential, intrinsically disordered proteins have generally been considered undruggable because of their lack of classical long-lived binding pockets for small molecules. Currently, only a few instances are known where small molecules have been observed to interact with intrinsically disordered proteins, and this situation is further exacerbated by the limited sensitivity of experimental techniques to detect such binding events. I will share our recent work which combines all-atom metadynamic simulations and nuclear magnetic resonance spectroscopy to characterise the interactions between small molecules and intrinsically disordered proteins towards the discovery and development of new therapeutics targeting these highly dynamic biomolecules.

Dividing cells in silico: how actin constricts the membrane – Ivan Palaia, King’s College London
To divide, our cells must generate coherent forces across their entire diameter. They do so by assembling nm-sized building blocks into a contractile ring, which pinches the cell membrane from the inside. How can such small building blocks produce reliable, coherent forces over distances of tens of µm? 

In this talk, we will build a minimal computational model to study the mechanics of cell division, involving actin filaments, molecular motors and a fluid membrane. After identifying the key principle behind a functional contractile ring, we will show that the constriction mechanism is robust against a plethora of perturbations, particularly in filament dynamics. This robustness may explain why this fundamental machinery has been conserved through evolution for over a billion years.

Palaia, Šarić, in preparation

Dar, Tesoro-Moreno, Palaia, Gopalan, Sun, Strauss, Sprenger, Belmonte, Foster, Murrell, Ejsing, Šarić, Leptin, Diz-Muñoz, bioRxiv:10.1101/2024.10.14.618153