A new model of chemical bonding in ionic melts.

We developed a new physical model to predict macroscopic properties of inorganic molten systems using a realistic description of inter-atomic interactions. Unlike the conventional approach, which tends to overestimate viscosity by several times, our systems consist of a set of ions with an admixture of neutral atoms. The neutral atom subsystem is a consequence of the covalent/ionic state reduction, occurring in the liquid phase.

The two-pathway model of the biological catch-bond as a limit of the allosteric model.

Catch-binding is a counterintuitive phenomenon in which the lifetime of a receptor/ligand bond increases when a force is applied to break the bond. Several mechanisms have been proposed to rationalize catch-binding. In the two-pathway model, the force drives the system away from its native dissociation pathway into an alternative pathway involving a higher energy barrier.

Regulation of catch binding by allosteric transitions.

An allosteric model is used to describe changes in lifetimes of biological receptor-ligand bonds subjected to an external force. Force-induced transitions between the two states of the allosteric site lead to changes in the receptor conformation. The ligand bound to the receptor fluctuates between two different potentials formed by the two receptor conformations.

Allosteric role of the large-scale domain opening in biological catch-binding.

The proposed model demonstrates the allosteric role of the two-domain region of the receptor protein in the increased lifetimes of biological receptor/ligand bonds subjected to an external force. The interaction between the domains is represented by a bounded potential, containing two minima corresponding to the attached and separated conformations of the two protein domains. The dissociative potential with a single minimum describing receptor/ligand binding fluctuates between deep and shallow states, depending on whether the domains are attached or separated.

Theoretical aspects of the biological catch bond.

The biological catch bond is fascinating and counterintuitive. When an external force is applied to a catch bond, either in vivo or in vitro, the bond resists breaking and becomes stronger instead. In contrast, ordinary slip bonds, which represent the vast majority of biological and chemical bonds, dissociate faster when subjected to a force.

Atomistic simulation combined with analytic theory to study the response of the P-selectin/PSGL-1 complex to an external force.

Steered molecular dynamics simulations are combined with analytic theory in order to gain insights into the properties of the P-selectin/PSGL-1 catch-slip bond at the atomistic level of detail. The simulations allow us to monitor the conformational changes in the P-selectin/PSGL-1 complex in response to an external force, while the theory provides a unified framework bridging the simulation data with experiment over 9 orders of magnitude. The theory predicts that the probability of bond dissociation by the catch mechanism is extremely low in the simulations; however, a few or even a single trajectory can be sufficient for characterization of the slip mechanism.

Correlation functions in quantized Hamilton dynamics and quantal cumulant dynamics.

Quantized Hamilton dynamics (QHD) [O. V. Prezhdo and Y.

Anomalously increased lifetimes of biological complexes at zero force due to the protein-water interface.

A number of biological bonds show dramatically increased lifetimes at zero-force conditions, compared to lifetimes when even a small tensile force is applied to the ligand. The discrepancy is so great that it cannot be explained by the traditional receptor-ligand binding models. This generic phenomenon is rationalized here by considering the interaction of water with the receptor-ligand complex.

Dissipation of classical energy in nonlinear quantum systems.

We show using two simple nonlinear quantum systems that the infinite set of quantum dynamical variables, as introduced in quantized Hamilton dynamics [O. V. Prezhdo and Y.

Universal laws in the force-induced unraveling of biological bonds.

Universal laws in the force-induced unbinding of receptor-ligand complexes are established for a general functional dependence of the dissociation rate constant on the applied force and are detailed with the two-pathway model that describes the recently discovered biological catch bond. The relationships link the data obtained with constant and time-dependent forces in different regimes, provide common representation for the previously unrelated data sets, and, thereby, greatly facilitate analysis and interpretation of experiments. The universal laws are demonstrated with the monomeric and dimeric catch-slip bonds between P-selectins and P-selectin glycoprotein ligands-1, and the slip bond between E-selectin and sialyl Lewis;{x} antigen.

Force-induced deformations and stability of biological bonds.

A deformation model of the forced-induced dissociation of biological bonds is developed. A simple illustration shows that protein deformations can change the receptor-ligand interaction linearly with applied force at small forces, either increasing or decreasing the bond stability, and that a minor external work can lead to notable changes in the interaction energy. The deformation-induced increase of bond stability is illustrated with the remarkable catch-bond phenomenon in P and L selections.

Dissociation of biological catch-bond by periodic perturbation.

The analysis of the P-selectin/PSGL-1 catch-slip bond that is periodically driven by a detaching force predicts that in the frequency range on the order of 1 s(-1) the bond lifetime undergoes significant changes with respect to both frequency and amplitude of the force. The result indicates how variations in the heart rate could have a substantial effect on leukocyte and lymphoid cell transport and adhesion to endothelial cells and platelets during inflammatory processes.

Distinctive features of the biological catch bond in the jump-ramp force regime predicted by the two-pathway model.

The receptor-ligand unbinding in the biological catch bond is analyzed within a simple model that comprises a single bound state and two unbinding pathways. This model is investigated in detail for the jump-ramp force regime, where the pulling force quickly jumps to a finite value and then is ramped linearly with time. Two qualitative criteria are identified that distinguish the catch bond from the slip bond.

The two-pathway model for the catch-slip transition in biological adhesion.

Some recently studied biological noncovalent bonds have shown increased lifetime when stretched by mechanical force. In each case these counterintuitive "catch-bonds" have transitioned into ordinary "slip-bonds" that become increasingly shorter lived as the tensile force on the bond is further increased. We describe analytically how these results are supported by a physical model whereby the ligand escapes the receptor binding site via two alternative routes, a catch-pathway that is opposed by the applied force and a slip-pathway that is promoted by force.

Macroscopic order and electro-optic response of dipolar chromophore-polymer materials.

This Minireview considers the key factors that govern the organization of macroscopic polarization in nonlinear optical systems obtained by electric poling of organic dipolar chromophores dissolved in polymer matrices. The macroscopic electric polarization depends on the thermodynamic state of the dipole system. The dependence of the paraelectric and antiferroelectric states of dipolar chromophores on the chromophore concentration and the strength of the poling field is discussed.