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Fabio Bruni

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3 published item(s)

preprint2026arXiv

Kin-ematic Exclusion in Active Matter: Modelling Mutual Inhibition in \textit{Pseudomonas aeruginosa} Sibling Colonies

The striking variety of macroscopic morphologies displayed by bacterial colonies depends on microscopic environmental and behavioural details in a manner that is currently not well understood. A surprising example is sibling inhibition, whereby isogenic bacterial colonies spreading in soft agar hydrogels tend to avoid each other and form sharp demarcation lines when growing nearby. Here we investigate this effect with the common pathogen \textit{Pseudomonas aeruginosa}, by combining quantitative density measurements with a minimal biophysical model. Our results show that the phenomenon does not depend on gel compression, lethal inhibition or quorum sensing-dependent cell communication. Instead, colony separation is driven by localised nutrient depletion through a dynamic feedback between growth and motility. The model, which is calibrated using experimental data, captures key observations including the dependence of inhibition strength on the initial nutrient concentration. This work establishes nutrient availability and non-lethal motility inhibition as central factors underlying sibling inhibition, providing a generalisable framework for microbial spatial dynamics with implications for understanding bacterial interactions in tissues, soils and engineered microbiomes.

preprint2011arXiv

More than one dynamic crossover in protein hydration water

Studies of liquid water in its supercooled region have led to many insights into the structure and behavior of water. While bulk water freezes at its homogeneous nucleation temperature of approximately 235 K, for protein hydration water, the binding of water molecules to the protein avoids crystallization. Here we study the dynamics of the hydrogen bond (HB) network of a percolating layer of water molecules, comparing measurements of a hydrated globular protein with the results of a coarse-grained model that has been shown to successfully reproduce the properties of hydration water. With dielectric spectroscopy we measure the temperature dependence of the relaxation time of protons charge fluctuations. These fluctuations are associated to the dynamics of the HB network of water molecules adsorbed on the protein surface. With Monte Carlo (MC) simulations and mean--field (MF) calculations we study the dynamics and thermodynamics of the model. In both experimental and model analyses we find two dynamic crossovers: (i) one at about 252 K, and (ii) one at about 181 K. The agreement of the experiments with the model allows us to relate the two crossovers to the presence of two specific heat maxima at ambient pressure. The first is due to fluctuations in the HB formation, and the second, at lower temperature, is due to the cooperative reordering of the HB network.

preprint2009arXiv

A new water anomaly: the temperature dependence of the proton mean kinetic energy

The mean kinetic energy of protons in water is determined by Deep Inelastic Neutron Scattering experiments, performed above and below the temperature of maximum density and in the supercooled phase. The temperature dependence of this energy shows an anomalous behavior, as it occurs for many water properties. In particular two regions of maximum kinetic energy are identified: the first one, in the supercooled phase in the range 269 K - 272 K, and a second one above 273 K. In both these regions the measured proton kinetic energy exceedes the theoretical prediction based on a semi-classical model. Noteworthy, the proton mean kinetic energy has a maximum at 277 K, the temperature of the maximum density of water. In the supercooled metastable phase the measured mean kinetic energy and the proton momentum distribution clearly indicate proton delocalization between two H-bonded oxygens.