Continuum Electrostatics Research Articles

Dielectric Boundary Force for the Minimization of the Mean-Field Electrostatic Free-Energy Functional Including the Ionic Size Effect

The generalized Poisson–Boltzmann equation with the uniform ionic size is investigated. In mean-field theory, the ionic size effect is added by modifying the entropy effect of solvent molecules in the electrostatic free-energy functional of ion concentrations. Taking minimization of the mean-field electrostatic free-energy functional including the ionic size effect with respect to the ion concentrations, the minimum free-energy is obtained (see (4.6) in Li [(2009a) “Continuum electrostatics for ionic solutions with non-uniform ionic sizes,” Nonlinearity 22(4), 811–833]. Maximizing the minimum free-energy with respect to the electrostatic potential determines the generalized Poisson–Boltzmann equation. By the definition of shape derivative, the first variation of this minimum free-energy with respect to variation of the dielectric boundary is derived. Thus, the dielectric boundary force of an ionic solution with multiple ionic species with the uniform ionic size is obtained.

Delineating redox cooperativity in water-soluble and membrane multiheme cytochromes through protein design.

Nature has evolved diverse electron transport proteins and multiprotein assemblies essential to the generation and transduction of biological energy. However, substantially modifying or adapting these proteins for user-defined applications or to gain fundamental mechanistic insight can be hindered by their inherent complexity. De novo protein design offers an attractive route to stripping away this confounding complexity, enabling us to probe the fundamental workings of these bioenergetic proteins and systems, while providing robust, modular platforms for constructing completely artificial electron-conducting circuitry. Here, we use a set of de novo designed mono-heme and di-heme soluble and membrane proteins to delineate the contributions of electrostatic micro-environments and dielectric properties of the surrounding protein medium on the inter-heme redox cooperativity that we have previously reported. Experimentally, we find that the two heme sites in both the water-soluble and membrane constructs have broadly equivalent redox potentials in isolation, in agreement with Poisson-Boltzmann Continuum Electrostatics calculations. BioDC, a Python program for the estimation of electron transfer energetics and kinetics within multiheme cytochromes, also predicts equivalent heme sites, and reports that burial within the low dielectric environment of the membrane strengthens heme-heme electrostatic coupling. We conclude that redox cooperativity in our diheme cytochromes is largely driven by heme electrostatic coupling and confirm that this effect is greatly strengthened by burial in the membrane. These results demonstrate that while our de novo proteins present minimalist, new-to-nature constructs, they enable the dissection and microscopic examination of processes fundamental to the function of vital, yet complex, bioenergetic assemblies.

Induced charges in a Thomas–Fermi metal: insights from molecular simulations

We study the charge induced in a Thomas–Fermi metal by an ion in vacuum, using an atomistic description employed in constant-potential molecular dynamics simulations, and compare the results with the predictions from continuum electrostatics. Specifically, we investigate the effects of the Thomas–Fermi screening length l TF and the position d of the ion with respect to the surface on the induced charge distribution in a graphite electrode. The continuum predictions capture most of the features observed with the atomistic description (except the oscillations due to the atomic sites of the graphite lattice), provided that d and l TF are larger than the inter-atomic distances within the electrode. At large radial distance from the ion, the finite l TF case can be well approximated by the solution for a perfect metal using an effective distance d + l TF . This requires a careful definition of the effective interface between the metal and vacuum for the continuum description. Our atomistic results support in particular an early analytical prediction (Vorotyntsev and Kornyshev, Sov. J. Exp. Theor. Phys. 51, 509 (Mar., 1980)) for a single charge at the interface between a Thomas–Fermi metal and a polarisable medium, which remains to be tested in atomistic simulations with an explicit solvent.

The oxidation of the [4Fe-4S] cluster of DNA primase alters the binding energies with DNA and RNA primers

DNA primase is an iron sulfur enzyme in DNA replication responsible for synthesizing short RNA primers that serve as starting points for DNA synthesis. The role of the [4Fe-4S] cluster is not well determined. Here, we calculate the redox potential of the [4Fe-4S] with and without DNA/RNA using continuum electrostatics. In addition, we identify the structural changes coupled to the oxidation/reduction. Our calculations show that the DNA/RNA primer lowers the redox potential by 110 and 50 mV for the [4Fe-4S]+ and [4Fe-4S]2+ states, respectively. The oxidation of the cluster is coupled to structural changes that significantly reduce the binding energies between the DNA and the nearby residues. The negative charges accumulated by the DNA and the RNA primers induce the oxidation of the [4Fe-4S] cluster. This in turn stimulates structural changes on the DNA-protein interface that significantly reduce the binding energies.

Computing the Relative Affinity of Chlorophylls a and b to Light-Harvesting Complex II.

In plants and algae, the primary antenna protein bound to photosystem II is light-harvesting complex II (LHCII), a pigment-protein complex that binds eight chlorophyll (Chl) a molecules and six Chl b molecules. Chl a and Chl b differ only in that Chl a has a methyl group (-CH3) on one of its pyrrole rings, while Chl b has a formyl group (-CHO) at that position. This blue-shifts the Chl b absorbance relative to Chl a. It is not known how the protein selectively binds the right Chl type at each site. Knowing the selection criteria would allow the design of light-harvesting complexes that bind different Chl types, modifying an organism to utilize the light of different wavelengths. The difference in the binding affinity of Chl a and Chl b in pea and spinach LHCII was calculated using multiconformation continuum electrostatics and free energy perturbation. Both methods have identified some Chl sites where the bound Chl type (a or b) has a significantly higher affinity, especially when the protein provides a hydrogen bond for the Chl b formyl group. However, the Chl a sites often have little calculated preference for one Chl type, so they are predicted to bind a mixture of Chl a and b. The electron density of the spinach LHCII was reanalyzed, which, however, confirmed that there is negligible Chl b in the Chl a-binding sites. It is suggested that the protein chooses the correct Chl type during folding, segregating the preferred Chl to the correct binding site.

Virtual Model Compound Approach for Calculating Redox Potentials of [Fe2S2]-Cys4 Centers in Proteins - Structure Quality Matters.

The midpoint potential of the [Fe2S2]-Cys4-cluster in proteins is known to vary between -200 and -450 mV. This variation is caused by the different electrostatic environment of the cluster in the respective proteins. Continuum electrostatics can quantify the impact of the protein environment on the redox potential. Thus, if the redox potential of a [Fe2S2]-Cys4-cluster model compound in aqueous solution would be known, then redox potentials in various protein complexes could be calculated. However, [Fe2S2]-Cys4-cluster models are not water-soluble, and thus, their redox potential can not be measured in aqueous solution. To overcome this problem, we introduce a method that we call Virtual Model Compound Approach (VMCA) to extrapolate the model redox potential from known redox potentials of proteins. We carefully selected high-resolution structures for our analysis and divide them into a fit set, for fitting the model redox potential, and an independent test set, to check the validity of the model redox potential. However, from our analysis, we realized that the some structures can not be used as downloaded from the PDB but had to be re-refined in order to calculate reliable redox potentials. Because of the re-refinement, we were able to significantly reduce the standard deviation of our derived model redox potential for the [Fe2S2]-Cys4-cluster from 31 mV to 10 mV. As the model redox potential, we obtained -184 mV. This model redox potential can be used to analyze the redox behavior of [Fe2S2]-Cys4-clusters in larger protein complexes.

Electrostatics-Based Computational Design and Experimental Analysis of Buforin II Antimicrobial Peptide Variants with Increased DNA Affinities.

Antimicrobial peptides (AMPs) are promising alternatives to traditional antibiotics in the treatment of bacterial infections in part due to their targeting of generic bacterial structures that make it more difficult to develop drug resistance. In this study, we introduce and implement a design workflow to develop more potent AMPs by improving their electrostatic interactions with DNA, which is a putative intracellular target. Using the existing membrane-translocating AMP buforin II (BF2) as a starting point, we use a computational workflow that integrates electrostatic charge optimization, continuum electrostatics, and molecular dynamics simulations to suggest peptide positions at which a neutral BF2 residue could be substituted with arginine to increase DNA-binding affinity either significantly or minimally, with the latter choice done to determine whether AMP binding affinity depends on charge distribution and not just overall monopole. Our analyses predicted that T1R and L8R BF2 variants would yield substantial and minimal increases in DNA-binding affinity, respectively. These predictions were validated with experimental peptide-DNA binding assays with additional computational analyses providing structural insights. Additionally, experimental measurements of antimicrobial potency showed that a design to increase DNA binding can also yield greater potency. As a whole, this study takes initial steps to support the idea that (i) a design strategy aimed to increase AMP binding affinity to DNA by focusing only on electrostatic interactions can improve AMP potency and (ii) the effect on DNA binding of increasing the overall peptide monopole via arginine substitution depends on the position of the substitution. More broadly, this design strategy is a novel way to increase the potency of other membrane-translocating AMPs that target nucleic acids.

Theoretical Interpretation of pH and Salinity Effect on Oil-in-Water Emulsion Stability Based on Interfacial Chemistry and Implications for Produced Water Demulsification

The petroleum industry produces thousands of barrels of oilfield waters from the initial stage driven by primary production mechanisms to the tertiary stage. These produced waters contain measurable amounts of oil-in-water emulsions, the exact amounts being determined by the chemistry of the crude oil. To meet strict environmental regulations governing the disposal of such produced waters, demulsification to regulatory permissible levels is required. Within the electric double layer theory, coupled with the analytical solutions to the Poisson–Boltzmann Equation, continuum electrostatics approaches can be used to describe the stability and electrokinetic properties of emulsions. In the literature, much of the surface charge density and zeta potential relationship to emulsion stability has been confined to systems with less salinity. In this paper, we have exploited the theoretical foundations of the electric double layer theory to carry out theoretical evaluations of emulsion salinity based on zeta potential and surface charge density calculations. Most importantly, our approaches have enabled us to extend such theoretical calculations to systems of the higher salinity characteristic of oil-in-water emulsions found in oilfield-produced waters, based on crude oil samples from the literature with varying surface chemistry. Moreover, based on the definition of acid crude oils, our choice of samples represents two distinct classes of crude oils. This approach enabled us to evaluate the stability of emulsions associated with these produced oilfield waters in addition to predicting the potential of demulsification using demulsifiers. Given that the salinity range of this study is that encountered with the vast majority of produced oilfield waters, the findings from our theoretical predictions are perfect guides as far as emulsion stability is concerned.

A thermodynamic relationship between the chemical equilibrium constant and the dielectric properties of the reaction medium: Solvent mixtures and universal solvents.

We introduce a novel thermodynamic model oriented toward accurately predicting the effect of solvent polarity on chemical equilibrium. Our approach is based on the fundamental principles of thermodynamics of continuum medium and can be applied generally to estimate the Gibbs free energy contribution resulting from electrostatic interactions between the solvent and chemical species to the corresponding equilibrium constant in the solution phase. Using a set of assumptions, we have developed a practical calculation methodology that employs multivariate fitting to determine the dependence of 27 different reactions, including tautomerizations, dimerizations, and acid-base dissociations, on solvent polarity. From this approach, we estimated all the contributions to the Gibbs free energy of reaction in the solution phase of some of these processes, including the gas phase Gibbs free energy of reaction, the electrostatic (continuum) contribution to the solvation Gibbs free of the involved solutes and, even, the Gibbs free energy contribution due to specific (intramolecular) solute-solvent interactions, albeit indirectly.

Insights into receptor structure and dynamics at the surface of living cells

Evaluating protein structures in living cells remains a challenge. Here, we investigate Interleukin-4 receptor alpha (IL-4Rα) into which the non-canonical amino acid bicyclo[6.1.0]nonyne-lysine (BCNK) is incorporated by genetic code expansion. Bioorthogonal click labeling is performed with tetrazine-conjugated dyes. To quantify the reaction yield in situ, we develop brightness-calibrated ratiometric imaging, a protocol where fluorescent signals in confocal multi-color images are ascribed to local concentrations. Screening receptor mutants bearing BCNK in the extracellular domain uncovered site-specific variations of both click efficiency and Interleukin-4 binding affinity, indicating subtle well-defined structural perturbations. Molecular dynamics and continuum electrostatics calculations suggest solvent polarization to determine site-specific variations of BCNK reactivity. Strikingly, signatures of differential click efficiency, measured for IL-4Rα in ligand-bound and free form, mirror sub-angstrom deformations of the protein backbone at corresponding locations. Thus, click efficiency by itself represents a remarkably informative readout linked to protein structure and dynamics in the native plasma membrane.

The Rate Constant - Reaction Free Energy Dependence for the Electron Transfer Reactions in Solutions. The Way to Interpret the Experimental Data Correctly

The relative influences of the reorganization energies of the classical and quantum modes on the maximum position of the rate constant – reaction free energy curve have been studied. In the framework of the continuum electrostatics, the electron transfer reorganization energies in methyltetrahydrofurane solutions for the system biphenylyl – spacer – acceptor were calculated. For different acceptors the solvent reorganization energy varies from 1.0 to 1.1 eV. When added with the rather small reorganization energies for classical intra-molecular modes we obtain 1.13 - 1.34 eV. With account of possible errors this coincides practically with the experimental estimate of the energy at the maximum of the rate–free energy curve DGmax ? -1.2 eV. Hence, we can conclude that the reorganization of quantum modes does not influence substantially the position of this maximum. To the contrary, in a non-polar solvent isooctane were the solvent reorganization does not play any role the reorganization of the quantum intra-reactants modes becomes determinant. These conclusions agree fully with the results of the general theoretical analysis and should be accounted for in the experimental data interpretation.

Computational Assessment of Protein-Protein Binding Specificity within a Family of Synaptic Surface Receptors.

Atomic-level information is essential to explain the formation of specific protein complexes in terms of structure and dynamics. The set of Dpr and DIP proteins, which play a key role in the neuromorphogenesis in the nervous system of Drosophila melanogaster, offer a rich paradigm to learn about protein-protein recognition. Many members of the DIP subfamily cross-react with several members of the Dpr family and vice versa. While there exists a total of 231 possible Dpr-DIP heterodimer complexes from the 21 Dpr and 11 DIP proteins, only 57 "cognate" pairs have been detected by surface plasmon resonance (SPR) experiments, suggesting that the remaining 174 pairs have low or unreliable binding affinity. Our goal is to assess the performance of computational approaches to characterize the global set of interactions between Dpr and DIP proteins and identify the specificity of binding between each DIP with their corresponding Dpr binding partners. In addition, we aim to characterize how mutations influence the specificity of the binding interaction. In this work, a wide range of knowledge-based and physics-based approaches are utilized, including mutual information, linear discriminant analysis, homology modeling, molecular dynamics simulations, Poisson-Boltzmann continuum electrostatics calculations, and alchemical free energy perturbation to decipher the origin of binding specificity of the Dpr-DIP complexes examined. Ultimately, the results show that those two broad strategies are complementary, with different strengths and limitations. Biological inter-relations are more clearly revealed through knowledge-based approaches combining evolutionary and structural features, the molecular determinants controlling binding specificity can be predicted accurately with physics-based approaches based on atomic models.

A Computational Study of the Promiscuity of the SAM-Dependent Methyltransferase AtHTMT1.

A two-pronged computational approach was taken to study the promiscuity of the SAM+-dependent methyl transferase AtHTMT1 from thale cress with several nucleophiles (Cl–, Br–, I–, NCO–, NCS–). First, enzyme-free methyl transfer reactions were studied with M05/6-311+G(2d,p) DFT calculations and electrostatic continuum models (PCM/SMD) for various chemical environments. Second, QM/MM MD simulations with semiempirical Hamiltonians (PM7, PM6-D3, AM1, PM6-D3H4) and the AMBER 14SB force field were used to study the enzyme catalyzed reaction in silico. The combination of the DFT and MD results shows that reactant desolvation generally accelerates the reaction, but it cannot explain the selectivity of the enzyme. The critical position of H2O molecules at the reactive site favors the reaction of NCS– over Cl– and Br– in agreement with experiments, but not observed in the quantum calculations for the cytosol. The addition of selected H2O molecules to the N terminus of NCS– greatly increases its reactivity, while H2O molecules attached to Cl– slow the reaction. The partial solvation of the nucleophiles in the reactive pouch holds the key to understanding the reactivity of AtHTMT1.

Computational Approach for Probing Redox Potential for Iron-Sulfur Clusters in Photosystem I.

Simple SummaryMany biological systems contain iron–sulfur clusters, which are typically found as components of electron transport proteins. Continuum electrostatic calculations were used to investigate the effect of protein environment on the redox properties of the three iron–sulfur clusters in the cyanobacterial photosystem I. Our results show a good correlation between the estimated and the measured reduction potential. Moreover, the results indicate that the low potential of FX is shown to be due to the interactions with the surrounding residues and ligating sulfurs. Our results will help in understanding the electron transfer reaction in photosystem I.Photosystem I is a light-driven electron transfer device. Available X-ray crystal structure from Thermosynechococcus elongatus showed that electron transfer pathways consist of two nearly symmetric branches of cofactors converging at the first iron–sulfur cluster FX, which is followed by two terminal iron–sulfur clusters FA and FB. Experiments have shown that FX has lower oxidation potential than FA and FB, which facilitates the electron transfer reaction. Here, we use density functional theory and Multi-Conformer Continuum Electrostatics to explain the differences in the midpoint potentials of the FX, FA and FB clusters. Our calculations show that FX has the lowest oxidation potential compared to FA and FB due to strong pairwise electrostatic interactions with surrounding residues. These interactions are shown to be dominated by the bridging sulfurs and cysteine ligands, which may be attributed to the shorter average bond distances between the oxidized Fe ion and ligating sulfurs for FX compared to FA and FB. Moreover, the electrostatic repulsion between the 4Fe-4S clusters and the positive potential of the backbone atoms is lowest for FX compared to both FA and FB. These results agree with the experimental measurements from the redox titrations of low-temperature EPR signals and of room temperature recombination kinetics.

A molecular perspective on induced charges on a metallic surface.

Understanding the response of the surface of metallic solids to external electric field sources is crucial to characterize electrode-electrolyte interfaces. Continuum electrostatics offer a simple description of the induced charge density at the electrode surface. However, such a simple description does not take into account features related to the atomic structure of the solid and to the molecular nature of the solvent and of the dissolved ions. In order to illustrate such effects and assess the ability of continuum electrostatics to describe the induced charge distribution, we investigate the behavior of a gold electrode interacting with sodium or chloride ions fixed at various positions, in a vacuum or in water, using all-atom constant-potential classical molecular dynamics simulations. Our analysis highlights important similarities between the two approaches, especially under vacuum conditions and when the ion is sufficiently far from the surface, as well as some limitations of the continuum description, namely, neglecting the charges induced by the adsorbed solvent molecules and the screening effect of the solvent when the ion is close to the surface. While the detailed features of the charge distribution are system-specific, we expect some of our generic conclusions on the induced charge density to hold for other ions, solvents, and electrode surfaces. Beyond this particular case, the present study also illustrates the relevance of such molecular simulations to serve as a reference for the designof improved implicit solvent models of electrode-electrolyte interfaces.

Prediction of multiple dry-wet transition pathways with a mesoscale variational approach.

Water fluctuates in a hydrophobic confinement, forming multiple dry and wet hydration states through evaporation and condensation. Transitions between such states are critical to both thermodynamics and kinetics of solute molecular processes, such as protein folding and protein-ligand binding and unbinding. To efficiently predict such dry-wet transition paths, we develop a hybrid approach that combines a variational implicit solvation model, a generalized string method for minimum free-energy paths, and the level-set numerical implementation. This approach is applied to three molecular systems: two hydrophobic plates, a carbon nanotube, and a synthetic host molecule Cucurbit[7]uril. Without an explicit description of individual water molecules, our mesoscale approach effectively captures multiple dry and wet hydration states, multiple dry-wet transition paths, such as those geometrically symmetric and asymmetric paths, and transition states, providing activation energy barriers between different states. Further analysis shows that energy barriers depend on mesoscopic lengths, such as the separation distance between the two plates and the cross section diameter of the nanotube, and that the electrostatic interactions strongly influence the dry-wet transitions. With the inclusion of solute atomic motion, general collective variables as reaction coordinates, and the finite-temperature string method, together with an improved treatment of continuum electrostatics, our approach can be further developed to sample an ensemble of transition paths, providing more accurate predictions of the transition kinetics.

Toward understanding the S2-S3 transition in the Kok cycle of Photosystem II: Lessons from Sr-substituted structure

Understanding the water oxidation mechanism in Photosystem II (PSII) stimulates the design of biomimetic artificial systems that can convert solar energy into hydrogen fuel efficiently. The Sr2+-substituted PSII is active but slower than with the native Ca2+ containing PSII as an oxygen evolving catalyst. Here, we use Density Functional Theory (DFT) to compare the energetics of the S2 to S3 transition in the Mn4O5Ca2+ and Mn4O5Sr2+ clusters. The calculations show that deprotonation of the water bound to Ca2+ (W3), required for the S2 to S3 transition, is energetically more favorable in Mn4O5Ca2+ than Mn4O5Sr2+. In addition, we have calculated the pKa of the water that bridges Mn4 and the Ca2+/Sr2+ in the S2 state using continuum electrostatics. The calculations show that the pKa is higher by 4 pH units in the Mn4O5Sr2+cluster.

Interplay of Interfacial Viscosity, Specific-Ion, and Impurity Adsorption Determines Zeta Potentials of Phospholipid Membranes.

Ion-specific induced changes of the ζ-potential of phospholipid vesicles are commonly used to quantify the affinity of different ions to the lipid interface. The negative ζ-potential of zwitterionic net-neutral phospholipid vesicles in neat water, which changes sign and increases in solutions of NaCl or KCl, is a phenomenon consistently observed in experiments but not fully understood theoretically. Using atomistic molecular dynamics simulations in the presence of applied electric fields which drive electroosmotic flows, in combination with an electrostatic continuum model based on the modified Poisson-Boltzmann and Helmholtz-Smoluchowski equations, we study the electrokinetic and electrostatic properties as well as the specific ion affinities to the phospholipid-water interface, in order to resolve these puzzling observations. Our modified continuum equations account for the dielectric profile at the lipid-water interface, ion-specific interactions between ions and the lipid-water interface, and the interfacial viscosity profile, which are all extracted from our atomistic simulations and rather accurately predict ion-density and electrostatic-potential distributions as well as ζ-potentials in comparison with our atomistic simulations. Our continuum model can explain experimental ζ-potentials only when we assume minute amounts of surface-active anionic impurities in the aqueous solution. In fact, the amount of impurities needed to explain the experimental data increases linearly with the salt concentration, suggesting that surface-active species, which might be already present in the lab water or lipid samples, could further be introduced through the added salt.

Proton exit pathways surrounding the oxygen evolving complex of photosystem II

Photosystem II allows water to be the primary electron source for the photosynthetic electron transfer chain. Water is oxidized to dioxygen at the Oxygen Evolving Complex (OEC), a Mn4CaO5 inorganic core embedded on the lumenal side of PSII. Water-filled channels surrounding the OEC must bring in substrate water molecules, remove the product protons to the lumen, and may transport the product oxygen. Three water-filled channels, denoted large, narrow, and broad, extend from the OEC towards the aqueous surface more than 15 Å away. However, the role of each pathway in the transport in and out of the OEC is yet to be established. Here, we combine Molecular Dynamics (MD), Multi Conformation Continuum Electrostatics (MCCE) and Network Analysis to compare and contrast the three potential proton transfer paths. Hydrogen bond network analysis shows that near the OEC the waters are highly interconnected with similar free energy for hydronium at all locations. The paths diverge as they move towards the lumen. The water chain in the broad channel is better connected than in the narrow and large channels, where disruptions in the network are observed approximately 10 Å from the OEC. In addition, the barrier for hydronium translocation is lower in the broad channel. Thus, a proton released from any location on the OEC can access all paths, but the likely exit to the lumen passes through PsbO via the broad channel.

Image-charge effects on ion adsorption near aqueous interfaces

Electrostatic interactions near surfaces and interfaces are ubiquitous in many fields of science. Continuum electrostatics predicts that ions will be attracted to conducting electrodes but repelled by surfaces with lower dielectric constant than the solvent. However, several recent studies found that certain "chaotropic" ions have similar adsorption behavior at air/water and graphene/water interfaces. Here we systematically study the effect of polarization of the surface, the solvent, and solutes on the adsorption of ions onto the electrode surfaces using molecular dynamics simulation. An efficient method is developed to treat an electrolyte system between two parallel conducting surfaces by exploiting the mirror-expanded symmetry of the exact image-charge solution. With neutral surfaces, the image interactions induced by the solvent dipoles and ions largely cancel each other, resulting in no significant net differences in the ion adsorption profile regardless of the surface polarity. Under an external electric field, the adsorption of ions is strongly affected by the surface polarization, such that the charge separation across the electrolyte and the capacitance of the cell is greatly enhanced with a conducting surface over a low-dielectric-constant surface. While the extent of ion adsorption is highly dependent on the electrolyte model (the polarizability of solvent and solutes, as well as the van der Waals radii), we find the effect of surface polarization on ion adsorption is consistent throughout different electrolyte models.