51 research outputs found
Evidence of a low-temperature dynamical transition in concentrated microgels
A low-temperature dynamical transition has been reported in several proteins.
We provide the first observation of a `protein-like' dynamical transition in
nonbiological aqueous environments. To this aim we exploit the popular
colloidal system of poly-N-isopropylacrylamide (PNIPAM) microgels, extending
their investigation to unprecedentedly high concentrations. Owing to the
heterogeneous architecture of the microgels, water crystallization is avoided
in concentrated samples, allowing us to monitor atomic dynamics at low
temperatures. By elastic incoherent neutron scattering and molecular dynamics
simulations, we find that a dynamical transition occurs at a temperature
~K, independently from PNIPAM mass fraction. However, the
transition is smeared out on approaching dry conditions. The quantitative
agreement between experiments and simulations provides evidence that the
transition occurs simultaneously for PNIPAM and water dynamics. The similarity
of these results with hydrated protein powders suggests that the dynamical
transition is a generic feature in complex macromolecular systems,
independently from their biological function
Water-polymer coupling induces a dynamical transition in microgels
The long debated protein dynamical transition was recently found also in
non-biological macromolecules, such as poly-N-isopropylacrylamide (PNIPAM)
microgels. Here, by using atomistic molecular dynamics simulations, we report a
description of the molecular origin of the dynamical transition in these
systems. We show that PNIPAM and water dynamics below the dynamical transition
temperature Td are dominated by methyl group rotations and hydrogen bonding,
respectively. By comparing with bulk water, we unambiguously identify
PNIPAM-water hydrogen bonding as the main responsible for the occurrence of the
transition. The observed phenomenology thus crucially depends on the
water-macromolecule coupling, being relevant to a wide class of hydrated
systems, independently from the biological function
Assembling patchy plasmonic nanoparticles with aggregation-dependent antibacterial activity
We realise an antibacterial nanomaterial based on the self-limited assembly
of patchy plasmonic colloids, obtained by adsorption of lysozyme to gold
nanoparticles. The possibility of selecting the size of the assemblies within
several hundred nanometres allows for tuning their optical response in a wide
range of frequencies from visible to near infrared. We also demonstrate an
aggregation-dependent modulation of the catalytic activity, which results in an
enhancement of the antibacterial performances for assemblies of the proper
size. The gained overall control on structure, optical properties and
biological activity of such nanomaterial paves the way for the development of
novel antibacterial nanozymes with promising applications in treating multi
drug resistant bacteria
Molecular origin of the two-step mechanism of gellan aggregation
Among hydrocolloids, gellan is one of the most studied polysaccharides due to its ability to form mechanically stable gels. Despite its long-standing use, the gellan aggregation mechanism is still not understood because of the lack of atomistic information. Here, we fill this gap by developing a new gellan force field. Our simulations offer the first microscopic overview of gellan aggregation, detecting the coil to single-helix transition at dilute conditions and the formation of higher-order aggregates at high concentration through a two-step process: first, the formation of double helices and then their assembly into superstructures. For both steps, we also assess the role of monovalent and divalent cations, complementing simulations with rheology and atomic force microscopy experiments and highlighting the leading role of divalent cations. These results pave the way for future use of gellan-based systems in a variety of applications, from food science to art restoration
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