Repulsive Intermolecular Forces Research Articles

The Effects of Short-Range Intermolecular Repulsive Forces on Hamaker Constant Estimation Using Atomic Force Microscopy.

The atomic force microscope (AFM), as it is able to characterize surface topography as well determine the AFM cantilever tip-surface force, proves effective at estimating the value of the Hamaker constant, A, for a given solid material. Two main AFM-based methods have been proposed for estimating values of A. In the approach-to-contact (AtC) method, Hamaker constants are inferred from the deflections at which the AFM tip first jumps into contact with the substrate. In the pull-off (PO) method, the deflections that arise when the AFM tip is finally pulled away from the substrate are used to estimate values of A. In prior applications of these two methods, the short-range intermolecular repulsive forces that are known to arise between the AFM tip and the substrate were, however, ignored. Upon invoking a physically relevant description of these short-range and steeply repulsive forces, we investigate the effects of repulsive interactions on the values of A estimated from the existing AtC and PO methods when applied to neutrally charged systems under low humidity or vacuum conditions. For experimentally relevant surfaces, we find that repulsive forces have a modest effect on the AtC method, although they still need to be accounted for in order to generate improved estimates of the Hamaker constant. On the other hand, repulsive forces have a significant effect on the Hamaker constants inferred from the PO method, and must be properly accounted for when using this approach. Our analysis also includes an explicit incorporation of surface roughness into the PO method, which is not typically done in most prior applications of the PO method.

The breakdown of the direct relation between the density scaling exponent of rotational dynamics and the intermolecular interaction potential for molecular systems with purely repulsive intermolecular forces

The breakdown of the direct relation between the density scaling exponent of rotational dynamics and the intermolecular interaction potential for molecular systems with purely repulsive intermolecular forces

The breakdown of the direct relation between the density scaling exponent and the intermolecular interaction potential for molecular systems with purely repulsive intermolecular forces

In this work, we question the generally accepted statement that the character of intermolecular interactions can be directly determined from the scaling exponent. We show that the scaling exponent evidently differs on the molecular architecture for pure inverse power law systems. Since these systems are characterized by a well-defined dependency between the intermolecular virial and potential energy, the results contradict theoretical predictions and previous reports. Moreover, we suggest that the recently proposed “molecular force” method also returns the value that varies from the one scaling the dynamics. Finally, the obtained result allows us to conclude that the value of the density scaling exponent for real liquids depends on intramolecular interactions.

Generic low-density corrections to the equation of state of chain molecules with repulsive intermolecular forces.

Molecular-based equations of state for describing the thermodynamics of chain molecules are often based on mean-field like arguments that reduce the problem of describing the interactions between chains to a simpler one involving only nonbonded monomers. While for dense liquids such arguments are known to work well, at low density they are typically less appropriate due to an incomplete description of the effect of chain connectivity on the local environment of the chains' monomer segments. To address this issue, we develop three semi-empirical approaches that significantly improve the thermodynamic description of chain molecules at low density. The approaches are developed for chain molecules with repulsive intermolecular forces; therefore, they could be used as reference models for developing equations of the state of real fluids based on perturbation theory. All three approaches are extensions of Wertheim's first-order thermodynamic perturbation theory (TPT1) for polymerization. The first model, referred to as TPT1-v, incorporates a second-virial correction that is scaled to zero at liquid-like densities. The second model, referred to as TPT1-y, introduces a Helmholtz-energy contribution to account for correlations between next-nearest-neighbor segments within chain molecules. The third approach, called TPT-E, directly modifies TPT1 without utilizing an additional Helmholtz energy contribution. By employing TPT1 at the core of these approaches, we ensure an accurate description of mixtures and enable a seamless extension from chains of tangentially bonded hard-sphere segments of equal size to hetero-segmented chains, fused chains, and chains of soft repulsive segments (which are influenced by temperature). The low-density corrections implemented in TPT1 are designed to preserve these good characteristics, as confirmed through comparisons with novel molecular simulation results for the pressure of various chain fluids. TPT1-v exhibits excellent transferability across different chain types, but it relies on knowing the second virial coefficient of the chain molecules, which is non-trivial to obtain and determined here using Monte Carlo simulation. The TPT1-y model, on the other hand, achieves comparable accuracy to TPT1-v while being fully predictive, requiring no input besides the geometry of the chain molecules.

Non-electrostatic interactions associated with aggregate formation between polyallylamine and Escherichia coli

Bacterial aggregation by mixing with polymers is applied as pretreatment to identify pathogens in patients with infectious diseases. However, the detailed interaction between polymers and bacteria has yet to be fully understood. Here, we investigate the interaction between polyallylamine and Escherichia coli by isothermal titration calorimetry. Aggregation was observed at pH 10 and the binding was driven by favorable enthalpic gain such as the electrostatic interaction. Neither aggregation nor the apparent heat of binding was observed at pH 4.0, despite the strong positive charge of polyallylamine. These results suggest that intermolecular repulsive forces of the abundant positive charge of polyallylamine cause an increased loss of conformational entropy by binding. Non-electrostatic interaction plays a critical role for aggregation.

Controlling the Self-Assembly and Material Properties of β-Sheet Peptide Hydrogels by Modulating Intermolecular Interactions.

Self-assembling peptides are a promising biomaterial with potential applications in medical devices and drug delivery. In the right combination of conditions, self-assembling peptides can form self-supporting hydrogels. Here, we describe how balancing attractive and repulsive intermolecular forces is critical for successful hydrogel formation. Electrostatic repulsion is tuned by altering the peptide's net charge, and intermolecular attractions are controlled through the degree of hydrogen bonding between specific amino acid residues. We find that an overall net peptide charge of +/-2 is optimal to facilitate the assembly of self-supporting hydrogels. If the net peptide charge is too low then dense aggregates form, while a high molecular charge inhibits the formation of larger structures. At a constant charge, altering the terminal amino acids from glutamine to serine decreases the degree of hydrogen bonding within the assembling network. This tunes the viscoelastic properties of the gel, reducing the elastic modulus by two to three orders of magnitude. Finally, hydrogels could be formed from glutamine-rich, highly charged peptides by mixing the peptides in combinations with a resultant net charge of +/-2. These results illustrate how understanding and controlling self-assembly mechanisms through modulating intermolecular interactions can be exploited to derive a range of structures with tuneable properties.

Electro-reversible adsorption as a versatile tool for the removal of diclofenac from wastewater

In this study, adsorption of a non-steroidal anti-inflammatory drug such as Diclofenac (DCF) on a commercial carbonaceous aerogel honeycomb monolith (NANOLIT®-NQ40) was ascertained. Based on, the overall design of an adsorption treatment should include a feasible regeneration process for the spent adsorbent. In this work, the adsorption/desorption process was ameliorated by coupling of electrochemical technology (anodic/cathodic polarisation). It was determined that the anodic polarisation enhanced the DCF removal and it was related with the applied voltage and the disposition of the electrodes into the bulk solution. Anodic polarisation at optimal conditions (voltage 0.9 V, electrodes gap 2.5 cm and electrolyte concentration higher than 1 mM) provoked an enhancement (around 30%) in the DCF adsorption rate. The spent aerogel regeneration method for the adsorbed or electro-adsorbed DCF was investigated and cathodic polarisation proved to be a viable regeneration alternative attaining the total regeneration of aerogel. The electro-desorption mechanism seemed to be linked to the generation of repulsive intermolecular forces in the aerogel surface. Finally, the sequential electro-adsorption/electro-desorption process was performed in successive cycles. The results confirmed the feasibility of this strategy, maintaining the efficiency with no structural changes in the monolith after several cycles being the electro-reversible adsorption of pollutants on aerogel a promising technology for the removal of pharmaceuticals from wastewater.

A Simple Principle for Understanding the Combined Cellular Protein Folding and Aggregation.

Proteins can undergo kinetic/thermodynamic partitioning between folding and aggregation. Proper protein folding and thermodynamic stability are crucial for aggregation inhibition. Thus, proteinfolding principles have been widely believed to consistently underlie aggregation as a consequence of conformational change. However, this prevailing view appears to be challenged by the ubiquitous phenomena that the intrinsic and extrinsic factors including cellular macromolecules can prevent aggregation, independently of (even with sacrificing) protein folding rate and stability. This conundrum can be definitely resolved by 'a simple principle' based on a rigorous distinction between protein folding and aggregation: aggregation can be controlled by affecting the intermolecular interactions for aggregation, independently of the intramolecular interactions for protein folding. Aggregation is beyond protein folding. A unifying model that can conceptually reconcile and underlie the seemingly contradictory observations is described here. This simple principle highlights, in particular, the importance of intermolecular repulsive forces against aggregation, the magnitude of which can be correlated with the size and surface properties of molecules. The intermolecular repulsive forces generated by the common intrinsic properties of cellular macromolecules including chaperones, such as their large excluded volume and surface charges, can play a key role in preventing the aggregation of their physically connected polypeptides, thus underlying the generic intrinsic chaperone activity of soluble cellular macromolecules. Such intermolecular repulsive forces of bulky cellular macromolecules, distinct from protein conformational change and attractive interactions, could be the puzzle pieces for properly understanding the combined cellular protein folding and aggregation including how proteins can overcome their metastability to amyloid fibrils in vivo.

Theoretical Study of Non-additive Hard Convex Body Fluid Mixtures

The structure of a dense fluid or liquid is largely determined by the repulsive intermolecular forces, so the hard core potential has been extensively employed to model real fluids and fluid mixtures. The properties of two dimensional hard body fluids and fluids mixtures have aroused a considerably interest in recent years. This is because they are treated as models of real fluids or fluid mixtures absorbed onto surfaces. The 2D hard-body fluids and fluid mixtures like their three-dimensional counter part are useful reference system in framing a perturbation theory for 2D real fluids and fluid mixtures of non-spherical molecules. The 2D hard-body systems are convex body (HCB) systems such as ellipse (HE) and hard discorectangles (HDR) and hard non-convex body systems i.e., fused hard discs (FHD) and planar hard dumbbell (HDB) systems. The equation of state of hard convex body fluid mixtures (HCB) is studied. Analytic expressions are given for the equation of state of the fluid mixture of the non-additive HCB. The numerical results are discussed for the non-additive hard dumbbell (HDB) fluid mixtures under different conditions for different values of non-additivity \(\Delta\). They depend on the conditions, shape parameters \(L^*_{11}\) and \(L^*_{22}\) , mole fractions \(x_1\) and \(x_2\) and \(\Delta\) in general and increase with the increase of packing fraction \(\Delta\).

Programmable Assembly of Peptide Amphiphile via Noncovalent-to-Covalent Bond Conversion.

Controlling the number of monomers in a supramolecular polymer has been a great challenge in programmable self-assembly of organic molecules. One approach has been to make use of frustrated growth of the supramolecular assembly by tuning the balance of attractive and repulsive intermolecular forces. We report here on the use of covalent bond formation among monomers, compensating for intermolecular electrostatic repulsion, as a mechanism to control the length of a supramolecular nanofiber formed by self-assembly of peptide amphiphiles. Circular dichroism spectroscopy in combination with dynamic light scattering, size-exclusion chromatography, and transmittance electron microscope analyses revealed that hydrogen bonds between peptides were reinforced by covalent bond formation, enabling the fiber elongation. To examine these materials for their potential biomedical applications, cytotoxicity of nanofibers against C2C12 premyoblast cells was tested. We demonstrated that cell viability increased with an increase in fiber length, presumably because of the suppressed disruption of cell membranes by the fiber end-caps.

A new approach for chemical reaction simulation of rarefied gas flow by DSMC method

Present study concerns the development of a new approach for chemical reaction modelling in DSMC technique. The conventional quantum-kinetic (QK) method based on the VHS collision model is usually applied by the DSMC algorithm to simulate chemical reactions in rarefied gas flowfield. In this paper, a modified quantum-kinetic model (MQK) is presented to remove some limitation of the QK chemical model. The MQK method uses the GSS collision model based on the Stockmayer potential function which can capture both the attractive and repulsive intermolecular forces and polarization effect of the molecules in the reactive flow. To investigate the accuracy and capability of the proposed model, firstly, dissociation of the nitrogen (non-polar gas) and water vapour (polar gas) are simulated in a single cell DSMC for equilibrium and non-equilibrium conditions. The results of the MQK are assessed with those of the QK methods, analytical models and experimental data. Secondly, dissociation of these two types of gases is studies in the rarefied gas flowfield along the stagnation line of a typical hypersonic atmospheric blunt body problem. The flowfield properties including the density, velocity, transient, vibrational and total temperature along the stagnation line and surface properties including the surface pressure and heatflux at the stagnation point obtained by the MQK model are compared with results of the QK method and available analytical and experimental data. The results show that the MQK model provides more accurate results when the polarization effects and both the attractive-repulsive intermolecular forces are dominant especially at high temperature. Also, comparison of the computational cost between two models indicates higher efficiency using the proposed method rather than the QK model due to reduction of number of the collision pairs.

Effect of polyethylene glycol conjugation on conformational and colloidal stability of a monoclonal antibody antigen-binding fragment (Fab').

We have investigated the effects of site specific "hinge" polyethylene glycol conjugation (PEGylation) on thermal, pH, and colloidal stability of a monoclonal antibody antigen-binding fragment (Fab') using a variety of biophysical techniques. The results obtained by circular dichroism (CD), ultraviolet (UV) absorbance, and fluorescence spectroscopy suggested that the physical stability of the Fab' is maximized at pH 6-7 with no apparent differences due to PEGylation. Temperature-induced aggregation experiments revealed that PEGylation was able to increase the transition temperature, as well as prevent the formation of visible and subvisible aggregates. Statistical comparison of the three-index empirical phase diagram (EPD) revealed significant differences in thermal and pH stability signatures between Fab' and PEG-Fab'. Upon mechanical stress, micro-flow imaging (MFI) and measurement of the optical density at 360 nm showed that the PEG-Fab' had significantly higher resistance to surface-induced aggregation compared to the Fab'. Analysis of the interaction parameter, kD, indicated repulsive intermolecular forces for PEG-Fab' and attractive forces for Fab'. In conclusion, PEGylation appears to protect Fab' against thermal and mechanical stress-induced aggregation, likely due to a steric hindrance mechanism.

Succinic acid in levels produced by yeast (Saccharomyces cerevisiae) during fermentation strongly impacts wheat bread dough properties

Succinic acid (SA) was recently shown to be the major pH determining metabolite produced by yeast during straight-dough fermentation (Jayaram et al., 2013), reaching levels as high as 1.6mmol/100g of flour. Here, the impact of such levels of SA (0.8, 1.6 and 2.4mmol/100g flour) on yeastless dough properties was investigated. SA decreased the development time and stability of dough significantly. Uniaxial extension tests showed a consistent decrease in dough extensibility upon increasing SA addition. Upon biaxial extension in the presence of 2.4mmol SA/100g flour, a dough extensibility decrease of 47–65% and a dough strength increase of 25–40% were seen. While the SA solvent retention capacity of flour increased with increasing SA concentration in the solvent, gluten agglomeration decreased with gluten yield reductions of over 50%. The results suggest that SA leads to swelling and unfolding of gluten proteins, thereby increasing their interaction potential and dough strength, but simultaneously increasing intermolecular electrostatic repulsive forces. These phenomena lead to the reported changes in dough properties. Together, our results establish SA as an important yeast metabolite for dough rheology.

Thermodynamic curvature for attractive and repulsive intermolecular forces

The thermodynamic curvature scalar R for the Lennard-Jones system is evaluated in phase space, including vapor, liquid, and solid state. We paid special attention to the investigation of R along vapor-liquid, liquid-solid, and vapor-solid equilibria. Because R is a measure of interaction strength, we traced out the line R=0 dividing the phase space into regions with effectively attractive (R<0) or repulsive (R>0) interactions. Furthermore, we analyzed the dependence of R on the strength of attraction applying a perturbation ansatz proposed by Weeks-Chandler-Anderson. Our results show clearly a transition from R>0 (for poorly repulsive interaction) to R<0 when loading attraction in the intermolecular potential.

“Magic” Surface Clustering of Borazines Driven by Repulsive Intermolecular Forces

“Magic” Surface Clustering of Borazines Driven by Repulsive Intermolecular Forces

“Magic” Surface Clustering of Borazines Driven by Repulsive Intermolecular Forces

It's a kind of magic: Hydroxy pentaaryl borazine molecules self-assemble into small clusters (see structure) on Cu(111) surfaces, whereas with symmetric hexaaryl borazine molecules large islands are obtained. Simulations indicate that the observed "magic" cluster sizes result from long-range repulsive Coulomb forces arising from the deprotonation of the B-OH groups of the hydroxy pentaaryl borazine.

Unravelling the nanometre-scale stimuli-responsive properties of natural rubber latex particles using atomic force microscopy

Natural rubber (NR) latex particles exhibit a core–shell structure, with a polyisoprene elastomer as the core and a thin layer made of proteins and lipids as the shell. Knowledge of the surface properties and interactions of core–shell NR particles is a key to gain a detailed understanding of their colloidal behaviour and to efficiently exploit them in industrial processes. Here, we report the first nanoscale measurement of the stimuli-responsive behaviour of single NR latex particles by atomic force microscopy (AFM), revealing that their molecular interactions are tightly controlled by salt conditions. High-resolution imaging, combined with protease treatments, confirmed the presence of a soft layer of proteins on the surface of the NR particles. Upon approach of the particles in diluted solutions of monovalent salts (1 mM NaCl), the AFM tip experienced a long-range repulsive force, reflecting electrostatic surface forces and compression of the soft, loosely structured protein layer. Upon retraction, sharp adhesion events were observed due to strong attractive interactions between the tip and proteins. When increasing the ionic strength (100 mM NaCl) or ion valency (1 mM and 100 mM MgCl2), the long-range repulsion was no longer seen, while nanotubes made of proteins and/or lipids were found to strengthen the tip–particle adhesive bonds. These findings, which correlate with the macroscopic aggregation of the particles, indicate that high ionic strength or ion valency leads to more compact shells by lowering repulsive intermolecular forces. The nanoscale measurements presented here provide new opportunities for quantifying the stimuli-responsive properties of soft colloids, like NR particles, and for tuning their interfacial interactions for industrial applications.

Cation Charge Dependence of the Forces Driving DNA Assembly

Understanding the strength and specificity of interactions among biologically important macromolecules that control cellular functions requires quantitative knowledge of intermolecular forces. Controlled DNA condensation and assembly are particularly critical for biology, with separate repulsive and attractive intermolecular forces determining the extent of DNA compaction. How these forces depend on the charge of the condensing ion has not been determined, but such knowledge is fundamental for understanding the basis of DNA-DNA interactions. Here, we measure DNA force-distance curves for a homologous set of arginine peptides. All forces are well fit as the sum of two exponentials with 2.4- and 4.8-Å decay lengths. The shorter-decay-length force is always repulsive, with an amplitude that varies slightly with length or charge. The longer-decay-length force varies strongly with cation charge, changing from repulsion with Arg 1 to attraction with Arg 2. Force curves for a series of homologous polyamines and the heterogeneous protein protamine are quite similar, demonstrating the universality of these forces for DNA assembly. Repulsive amplitudes of the shorter-decay-length force are species-dependent but nearly independent of charge within each species. A striking observation was that the attractive force amplitudes for all samples collapse to a single curve, varying linearly with the inverse of the cation charge.

About the physical validity of attaching the repulsive terms of analytical EOS models by temperature dependencies

This study demonstrates that any temperature dependency introduced in the term describing the inter-molecular repulsive forces of analytical EOS models leads to prediction of the infinite value for the isochoric heat capacity at the density limit conditions. The temperature-dependent hard sphere diameters and co-volumes necessarily result in the non-physical negative infinite values of this property at the infinite pressure, which in turn leads to the non-physical predictions of other properties, such as the sound velocities. In addition, this study demonstrates that the inconsistency existing at the imaginary state of infinite pressure may have a very strong negative impact on predicting the data of real fluids at the experimentally available pressures. Therefore making the repulsion compressibility factor temperature-dependent seems highly non-recommended.

Additional Supra-Self-Assembly of Human Serum Albumin under Amyloid-Like-Forming Solution Conditions

Protein aggregation has a multitude of consequences ranging from affecting protein expression to its implication in different diseases. Of recent interest is the specific form of aggregation leading to the formation of amyloid fibrils, structures associated with diseases such as Alzheimer's disease. These fibrils can further associate in other more complex structures such as fibrillar gels, plaques, or spherulitic structures. In the present work, we describe the physical and structural properties of additional supraself-assembled structures of human serum albumin under solution conditions in which amyloid-like fibrils are formed. We have detected the formation of ordered aggregates of amyloid fibrils, i.e., spherulites which possess a radial arrangement of the fibrils around a disorganized protein core and sizes of several micrometers by means of polarized optical microscopy, laser confocal microscopy, and transmission electron microscopy. These spherulites are detected both in solution and embedded in an isotropic matrix of fibrillar gels. In this regard, we have also noted the formation of protein gels when the protein concentration and/or ionic strength exceds a threshold value (the gelation point) as observed by rheometry. Fibrillar gels are formed through intermolecular nonspecific association of amyloid fibrils at a pH far away from the isolectric point of the protein where protein molecules seem to display a "solid-like" behavior due to the existence of non-DLVO (Derjaguin-Landau-Verwey-Overbeck) intermolecular repulsive forces. As the solution ionic strength increases, a coarsening of this type of gel is observed by environmental scanning microscopy. In contrast, at pH close to the protein isoelectric point, particulate gels are formed due to a faster aggregation process, which does not allow substantial structural reorganization to enable the formation of ordered structures. This behavior also additionally corroborates that the existence of particulates might also be a generic property of all polypeptide chains as amyloid fibril formation under suitable conditions.