Surface-controlled spatially heterogeneous physical properties of a supramolecular gel with homogeneous chemical composition

Controlling supramolecular self-assembly across multiple length scales to prepare gels with localised properties is challenging. Most strategies concentrate on fabricating gels with heterogeneous components, where localised properties are generated by the stimuli-responsive component. Here, as an alternative approach, we use a spiropyran-modified surface that can be patterned with light. We show that light-induced differences in surface chemistry can direct the bulk assembly of a low molecular weight gelator, 2-NapAV, meaning that mechanical gel properties can be controlled by the surface on which the gel is grown. Using grazing incidence X-ray diffraction and grazing incidence small angle X-ray scattering, we demonstrate that the origin of the different gel properties relates to differences in the architectures of the gels. This provides a new method to prepare a single domain (i.e., chemically homogeneous) hydrogel with locally controlled (i.e., mechanically heterogeneous) properties.

A mechanical pattern is created in a hydrogel film by pre-patterning the underlying surface chemistry. This allows spatial variation of the viscous component of the gel, controlling dissipative forces in the gel film without altering gel chemistry.     

Collaborate,compete and share

We introduce and study a model of an interacting population of agents who collaborate in groups which compete for limited resources. Groups are formed by random matching agents and their worth is determined by the sum of the efforts deployed by agents in group formation. Agents, on their side, have to share their effort between contributing to their group’s chances to outcompete other groups and resource sharing among partners, when the group is successful. A simple implementation of this strategic interaction gives rise to static and evolutionary properties with a very rich phenomenology. A robust emerging feature is the separation of the population between agents who invest mainly in the success of their group and agents who concentrate in getting the largest share of their group’s profits.     

Near-infrared Photoinactivation of Bacteria and Fungi at Physiologic Temperatures

We examined a laser system (870 and 930 nm), employing wavelengths that have exhibited cellular photodamage properties in optical traps. In vitro , with 1.5 cm diameter flat-top projections (power density of 5.66 W cm⁻²), at physiologic temperatures, we achieved photoinactivation of Staphylococcus aureus , Escherichia coli , Candida albicans and Trichophyton rubrum . Using nonlethal dosimetry, we measured a decrease in trans-membrane potentials (ΔΨmt and ΔΨp) and an increase in reactive oxygen species (ROS) generation in methicillin-resistant S. aureus (MRSA), C .  albicans and human embryonic kidney cells. We postulate that these multiplexed wavelengths cause an optically mediated mechano-transduction of cellular redox pathways, decreasing ΔΨ and increasing ROS. The cellular energetics of prokaryotic and fungal pathogens, along with mammalian cells, are affected in a similar manner when treated with these multiplexed wavelengths at the power densities employed. Following live porcine thermal tolerance skin experiments, we then performed human pilot studies, examining photodamage to MRSA in the nose and fungi in onychomycosis. No observable damage to the nares or the nail matrix was observed, yet photodamage to the pathogens was achieved at physiologic temperatures. The selective aspect of this near-infrared photodamage presents the possibility for its future utilization in human cutaneous antimicrobial therapy.     

Free energy for protein folding from nonequilibrium simulations using the Jarzynski equality

The equilibrium free energy difference between two long-lived molecular species or "conformational states" of a protein (or any other molecule) can in principle be estimated by measuring the work needed to shuttle the system between them, independent of the irreversibility of the process. This is the meaning of the Jarzynski equality (JE), which we test in this paper by performing simulations that unfold a protein by pulling two atoms apart. Pulling is performed fast relative to the relaxation time of the molecule and is thus far from equilibrium. Choosing a simple protein model for which we can independently compute its equilibrium properties, we show that the free energy can be exactly and effectively estimated from nonequilibrium simulations. To do so, one must carefully and correctly determine the ensemble of states that are pulled, which is more important the farther from equilibrium one performs simulations; this highlights a potential problem in using the JE to extract the free energy from forced unfolding experiments. The results presented here also demonstrate that the free energy difference between the native and denatured states of a protein measured in solution is not always equal to the free energy profile that can be estimated from forced unfolding simulations (or experiments) using the JE.     

Energies and spatial features for the rotationless bound states of 4He3+(2Sigmag+): a cationic core from helium cluster ionization

Ab initio quantum calculations have been carried out on the helium ionic trimer. The potential energy surface is accurately fitted, especially in the vicinity of the three equivalent minima. The spectrum of bound states for the zero angular momentum is computed and analyzed in detail. Energies and wave functions reveal several interesting features related to the fact that He3+ represents one of the few homonuclear ionic trimers that are linear in their ground vibrational state. At low energies, the triply degenerate eigenfunctions are localized at the potential minimum. With growing excitation energy, however, the wave functions exhibit stronger spatial delocalization.     

Direct spectroscopic evidence for competition between thermal molecular agitation and magnetic field in a tetrameric protein in aqueous solution

Samples of a typical tetrameric protein, the hemoglobin, at the concentration of 150 mg/ml in bidistilled water solution, were exposed to a uniform magnetic field at 200 mT at different temperatures of ${15}^{°}\text{C}$, ${40}^{°}\text{C}$ and ${65}^{°}\text{C}$. Fourier Transform Infrared Spectroscopy was used to analyze the response of the secondary structure of the protein to both stress agents, heating and static magnetic field. The most relevant result which was observed was the significant increasing in intensity of the Amide I band after exposure to the uniform magnetic field at the room temperature of ${15}^{°}\text{C}$. This result can be explained assuming that protein's α-helices aligned along the direction of the applied magnetic field due to their large dipole moment, inducing the alignment of the entire protein. Increasing of temperature up to ${40}^{°}\text{C}$ and ${65}^{°}\text{C}$ induced a significant reduction of the increasing in intensity of the Amide I band. This effect may be easily explained assuming that Brownian motion of the protein in water solution caused by thermal molecular agitation increased with increasing of temperature, contrasting the effect of the torque of the magnetic field applied to the protein in water solution.