Nonspecific Electrostatic Attraction Research Articles

Metastable nano-zirconium phosphate inside gel-type ion exchanger for enhanced removal of heavy metals

Nanotechnology has provided a new opportunity for water decontamination from trace heavy metals, yet the relatively poor acidic stability remains a major obstacle for the nano-adsorbents, given that acidic treatment is frequently used to regenerate the heavy metal-saturated adsorbents. Zirconium phosphate (ZrP) is very promising for water treatment due to its absolute insoluble nature, though it interacts with heavy metals mainly through the non-specific electrostatic attraction. Herein, we prepared the ultrafine ZrP (~3.9 nm) inside the commercially available gel-type cation exchanger (N001), i.e., the sulfonated poly(styrene-co-divinylbenzene) bead. The resultant nanocomposite ZrP@N001 contained the amorphous nanoparticles (NPs) with metastable γ-ZrP structure as the main phase, unlike the layered α-ZrP formed inside the macroporous cation exchanger D001 (referred to as ZrP@D001). As a result, ZrP@N001 could selectively adsorb heavy metals through inner-sphere coordination, possessing a much stronger adsorption affinity than ZrP@D001, as confirmed by XPS analysis. In both batch and column assays on the Pb(II)-polluted water, ZrP@N001 exhibited superior adsorption performance over ZrP@D001. After adsorption, the exhausted ZrP@N001 was fully refreshed by acidic treatment for a 5-cyclic adsorption-regeneration run with constant removal efficiencies. This study may open a door for the rational design of highly efficient water purifiers for heavy metal control.

Molecular Dynamics Study of Membrane Binding Mechanism of a Peripheral Membrane Protein OSH4

Oxysterol-binding protein -related proteins play major role in sterol and lipid transport via a non-vesicular pathway between cellular organelles. Osh4 is the most abundantly expressed member among seven homologue oxysterol binding proteins (OSH) in yeast. It is a peripheral membrane protein and its biological function is still not well understood. The binding mechanism of Osh4 towards various cellular membranes is crucial for its efficient biological function. Previous studies indicated six different membrane binding regions of Osh4 and identified non-specific electrostatic attractions between the membrane and the protein as the guiding factor for its membrane attachment. In this study, using a modified protein force field (CHARMM36m) and more accurate description for lipid-protein electrostatic interactions (CUFIX), we have investigated how the binding mechanism of Osh4 is affected by these new force field parameters using microsecond long all-atom molecular dynamics simulations. Our study indicates that the presence of negatively charged lipids in model membrane facilitates the initial contact between the membrane and the protein via non-specific electrostatic attraction. Furthermore, penetration of the phenylalanine loop in membrane is the crucial step for its stable membrane attachment. Once the phenylalanine loop anchors itself deeply in the membrane; the other regions of the Osh4 maximizes its contact with the membrane. Quantitative estimation of binding energies reveals that the hydrophobic attraction between the membrane and the protein is the main driving force for its stable membrane attachment. This varies from our past work that showed salt bridges stabilized Osh4-membrane contact.

Mimicking the graphene oxide structure in solutions by interaction of Fe(III) and Gd(III) with model small-size ligands. The NMR relaxation study

Despite long history and recent progress, the chemical behavior of graphene oxide (GO) is not fully understood. One of the remaining open questions is an extremely high cation exchange capacity, which cannot be explained in the frames of the commonly accepted Lerf-Klinowski structural model. The interaction of GO with metals, termed as sorption, is usually considered as physisorption, or as non-specific electrostatic attraction. Recently, we demonstrated that in fact this interaction has the coordinate-covalent bonding nature. In this work, by the means of the NMR relaxation, we investigated the interaction of Fe(III) and Gd(III) ions with several small molecule size chelators and with linear polymers in order to possibly mimic the GO structure. The experiments were conducted in the broad pH range, and at the different metal/chelator ratios. From the two tested metal ions, Fe(III) has the stronger affinity toward GO due to its higher charge density. GO binds Fe(III) with formation of strong high-relaxivity complexes, which do not undergo hydrolysis even in basic conditions. Numerous model small-size molecules, tested to mimic the GO structure, did not demonstrate the same effect on the relaxation of the Fe(III) and Gd(III) solutions, as does interaction with GO. From the tested linear polymers, only polyacrylic acid (PAA) can bind Fe(III), however, even PAA, consisting from carboxyl groups, cannot prevent Fe(III) from hydrolysis already in neutral solutions. Subsequently, carboxyl groups were excluded from the species in GO structure, responsible for the strong binding of meatal ions. We conclude that there are no preexisting sites or functional group fragments in GO structure, capable to strongly bind transition metal cations. The binding sites are formed from the existing structure upon the reaction with metal cations, to afford formation of the metal/GO coordination compounds. The most probable change in the GO structure is the formation of enolates from tertiary alcohols with rupture of the CC bonds. The newly reported data provide additional experimental evidence for the Dynamic Structural Model of GO and broadens the areas of its applicability.

Metastable Zirconium Phosphate under Nanoconfinement with Superior Adsorption Capability for Water Treatment

AbstractIn confined space with length scale of several nanometers, the phase behavior of matter, e.g., nucleation and crystallization, is completely different from its analogue in bulk. However, in environmental applications, the relationship between the nanoconfined crystallization behavior of inorganic crystals and their properties for pollutant removal is rarely elucidated. Herein, an unusual formation of zirconium phosphate (ZrP) crystals as a mixture of both thermodynamically stable α‐ and metastable γ‐phases inside the nanoconfinement of 7.9 nm pores of mesoporous polystyrene (MPS) is reported. This consequently changes the interaction between ZrP and toxic metal cations from nonspecific electrostatic attraction of normal α‐ZrP to highly specific inner‐sphere coordination of nanoconfined γ‐ZrP, which exhibits remarkable reactivity as well as reusability for the removal of toxic metals. The results of this study contribute to a better understanding of the use of nanoconfinement for the regulation of material properties.

Intrinsically disordered caldesmon binds calmodulin via the “buttons on a string” mechanism

We show here that chicken gizzard caldesmon (CaD) and its C-terminal domain (residues 636–771, CaD136) are intrinsically disordered proteins. The computational and experimental analyses of the wild type CaD136 and series of its single tryptophan mutants (W674A, W707A, and W737A) and a double tryptophan mutant (W674A/W707A) suggested that although the interaction of CaD136 with calmodulin (CaM) can be driven by the non-specific electrostatic attraction between these oppositely charged molecules, the specificity of CaD136-CaM binding is likely to be determined by the specific packing of important CaD136 tryptophan residues at the CaD136-CaM interface. It is suggested that this interaction can be described as the “buttons on a charged string” model, where the electrostatic attraction between the intrinsically disordered CaD136 and the CaM is solidified in a “snapping buttons” manner by specific packing of the CaD136 “pliable buttons” (which are the short segments of fluctuating local structure condensed around the tryptophan residues) at the CaD136-CaM interface. Our data also show that all three “buttons” are important for binding, since mutation of any of the tryptophans affects CaD136-CaM binding and since CaD136 remains CaM-buttoned even when two of the three tryptophans are mutated to alanines.

Directed synthesis of bio-inorganic vanadium oxide composites using genetically modified filamentous phage

The growth of crystalline vanadium oxide using a filamentous bacteriophage template was investigated using sequential incubation in a V2O5 precursor. Using the genetic modification of the bacteriophage, we displayed two cysteines that constrained the RSTB-1 peptide on the major coat protein P8, resulting in vanadium oxide crystallization. The phage-driven vanadium oxide crystals with different topologies, microstructures, photodegradation and vanadium oxide composites were characterized by scanning electron microscopy (SEM), transmission electron microscopy (TEM), quartz microbalance and dissipation (QCM-D) and X-ray photoelectron spectroscopy (XPS). Non-specific electrostatic attraction between a wild-type phage (wt-phage) and vanadium cations in the V2O5 precursor caused phage agglomeration and fiber formation along the length of the viral scaffold. As a result, the addition of recombinant phage (re-phage) in V2O5 precursors formed heterogeneous structures, which led to efficient condensation of vanadium oxide crystal formation in lines, shown by QCM-D analysis. Furthermore, re-phage/VxOx composites showed significantly enhanced photodegradation activities compared with the synthesized wt-phage-V2O5 composite under illumination. This study demonstrates that peptide-mediated vanadium oxide mineralization is governed by a complicated interplay of peptide sequence, local structure, kinetics and the presence of a mineralizing aid, such as the two cysteine-constrained peptides on the phage surface, and has potential for use in nanotechnology applications.

Phage-directed synthesis of copper sulfide: structural and optical characterization

The growth of crystalline copper sulfide using a viral template was investigated using sequential incubation in CuCl2 and Na2S precursors. Non-specific electrostatic attraction between a genetically-modified M13 bacteriophage and copper cations in the CuCl2 precursor caused phage agglomeration and bundle formation. Following the addition of Na2S, polydisperse nanocrystals 2–7 nm in size were found along the length of the viral scaffold. The structure of the copper sulfide material was identified as cubic anti-fluorite type Cu1.8S, space group . Strong interband absorption was observed within the ultraviolet to visible range with an onset near 800 nm. Furthermore, free carrier absorption, associated with the localized surface plasmon resonance of the copper sulfide nanocrystals, was seen in the near infrared with absorbance maxima at 1060 nm and 3000 nm, respectively.

Active Site Binding and Catalytic Role of Bicarbonate in 1,4-Dihydroxy-2-naphthoyl Coenzyme A Synthases from Vitamin K Biosynthetic Pathways

1,4-Dihydroxy-2-naphthoyl coenzyme A (DHNA-CoA) synthase, or MenB, catalyzes a carbon-carbon bond formation reaction in the biosynthesis of both vitamin K1 and K2. Bicarbonate is crucial to the activity of a large subset of its orthologues but lacks a clearly defined structural and mechanistic role. Here we determine the crystal structure of the holoenzymes from Escherichia coli at 2.30 Å and Synechocystis sp. PCC6803 at 2.04 Å, in which the bicarbonate cofactor is bound to the enzyme active site at a position equivalent to that of the side chain carboxylate of an aspartate residue conserved among bicarbonate-insensitive DHNA-CoA synthases. Binding of the planar anion involves both nonspecific electrostatic attraction and specific hydrogen bonding and hydrophobic interactions. In the absence of bicarbonate, the anion binding site is occupied by a chloride ion or nitrate, an inhibitor directly competing with bicarbonate. These results provide a solid structural basis for the bicarbonate dependence of the enzymatic activity of type I DHNA-CoA synthases. The unique location of the bicarbonate ion in relation to the expected position of the substrate α-proton in the enzyme's active site suggests a critical catalytic role for the anionic cofactor as a catalytic base in enolate formation.

Structural basis for solute transport, nucleotide regulation, and immunological recognition of Neisseria meningitidis PorB

PorB is the second most prevalent outer membrane protein in Neisseria meningitidis. PorB is required for neisserial pathogenesis and can elicit a Toll-like receptor mediated host immune response. Here, the x-ray crystal structure of PorB has been determined to 2.3 A resolution. Structural analysis and cocrystallization studies identify three putative solute translocation pathways through the channel pore: One pathway transports anions nonselectively, one transports cations nonselectively, and one facilitates the specific uptake of sugars. During infection, PorB likely binds host mitochondrial ATP, and cocrystallization with the ATP analog AMP-PNP suggests that binding of nucleotides regulates these translocation pathways both by partial occlusion of the pore and by restricting the motion of a putative voltage gating loop. PorB is located on the surface of N. meningitidis and can be recognized by receptors of the host innate immune system. Features of PorB suggest that Toll-like receptor mediated recognition outer membrane proteins may be initiated with a nonspecific electrostatic attraction.

Adsorption behavior of humic acid onto polypyrrole-coated nylon 6,6 granules

One of the challenges in water supply is the removal of humic substances as the unit treatment processes in a conventional water treatment plant are usually not effective for this purpose. In this study, nylon 6,6 granules were surface-modified by chemical polymerization of pyrrole and were used as a granular adsorbent for removing humic acid from water. Zeta potential study showed that the coated granules have positive surface charges over a wide range of pH values. X-Ray photoelectron spectroscopy (XPS) indicated that the positive surface charges of the coated granules are attributed to the protonated nitrogen atoms (i.e. N+) in the polypyrrole (PPy) coating. Batch adsorption experiments were conducted under various conditions to examine the removal efficiency and mechanisms. PPy-coated nylon 6,6 granules were found to have much better removal of humic acid, as compared to the uncoated nylon 6,6 granules, suggesting the importance of electrostatic interactions between the positively charged granules and the negatively charged humic acid in the process. Evidence showed that although most adsorption may take place through non-specific electrostatic attraction, some adsorption occurred at specific sites and resulted in charge neutralization. It was found that low pH and high ionic concentration favored the adsorption performance and the adsorption kinetics involved both diffusion-controlled and attachment-controlled mechanisms.

Effects of magnesium ions on the stabilization of RNA oligomers of defined structures.

Optical melting was used to determine the stabilities of 11 small RNA oligomers of defined secondary structure as a function of magnesium ion concentration. The oligomers included helices composed of Watson-Crick base pairs, GA tandem base pairs, GU tandem base pairs, and loop E motifs (both eubacterial and eukaryotic). The effect of magnesium ion concentration on stability was interpreted in terms of two simple models. The first assumes an uptake of metal ion upon duplex formation. The second assumes nonspecific electrostatic attraction of metal ions to the RNA oligomer. For all oligomers, except the eubacterial loop E, the data could best be interpreted as nonspecific binding of metal ions to the RNAs. The effect of magnesium ions on the stability of the eubacterial loop E was distinct from that seen with the other oligomers in two ways. First, the extent of stabilization by magnesium ions (as measured by either change in melting temperature or free energy) was three times greater than that observed for the other helical oligomers. Second, the presence of magnesium ions produces a doubling of the enthalpy for the melting transition. These results indicate that magnesium ion stabilizes the eubacterial loop E sequence by chelating the RNA specifically. Further, these results on a rather small system shed light on the large enthalpy changes observed upon thermal unfolding of large RNAs like group I introns. It is suggested that parts of those large enthalpy changes observed in the folding of RNAs may be assigned to variations in the hydration states and types of coordinating atoms in some specifically bound magnesium ions and to an increase in the observed cooperativity of the folding transition due to the binding of those magnesium ions coupling the two stems together. Brownian dynamic simulations, carried out to visualize the metal ion binding sites, reveal rather delocalized ionic densities in all oligomers, except for the eubacterial loop E, in which precisely located ion densities were previously calculated.

Sorption-desorption of ionogenic compounds at the mineral-water interface: study of metal oxide-rich soils and pure-phase minerals.

Sorption of the ionic compounds 2,4-D and quinmerac onto iron oxide-rich, variable charged soils was strongly influenced by mineralogy, particularly soil iron and aluminum oxides, whereas sorption of the neutral norflurazon was only related to total soil C. An appreciable fraction of the mass sorbed in stirred-flow studies was easily desorbed by deionized water, and desorption of ionic compounds was initially more rapid than sorption. This sorption-desorption behavior, although contrary to desorption hysteresis commonly observed in batch studies, suggests that the reversibly sorbed fraction is weakly bound to the soil surface. 2,4-D sorption to iron oxide-rich soils and pure-phase metal oxides appears to be driven by nonspecific electrostatic attraction, with specific electrostatic attraction and van der Waals interactions being secondary. Both the carboxylate and the heterocyclic N groups may participate in sorption of quinmerac, facilitated by specific and nonspecific electrostatic attraction and surface complexation. The heterocyclic N, amine, and carbonyl groups of norflurazon do not appear to interact with soil minerals.

Free Energy Landscapes of Encounter Complexes in Protein-Protein Association

We report the computer generation of a high-density map of the thermodynamic properties of the diffusion-accessible encounter conformations of four receptor-ligand protein pairs, and use it to study the electrostatic and desolvation components of the free energy of association. Encounter complex conformations are generated by sampling the translational/rotational space of the ligand around the receptor, both at 5-Å and zero surface-to-surface separations. We find that partial desolvation is always an important effect, and it becomes dominant for complexes in which one of the reactants is neutral or weakly charged. The interaction provides a slowly varying attractive force over a small but significant region of the molecular surface. In complexes with no strong charge complementarity this region surrounds the binding site, and the orientation of the ligand in the encounter conformation with the lowest desolvation free energy is similar to the one observed in the fully formed complex. Complexes with strong opposite charges exhibit two types of behavior. In the first group, represented by barnase/barstar, electrostatics exerts strong orientational steering toward the binding site, and desolvation provides some added adhesion within the local region of low electrostatic energy. In the second group, represented by the complex of kallikrein and pancreatic trypsin inhibitor, the overall stability results from the rather nonspecific electrostatic attraction, whereas the affinity toward the binding region is determined by desolvation interactions.

Calcium and Sulfate Retention by Two Oxisols of the Brazilian Cerrado

AbstractThe ability of two representative oxisols from the Cerrado region of Brazil to adsorb Ca2+ and SO2‐4, when in their natural acidic state, was determined by using dissolved CaCl2, K2SO4 and CaSO4 salts as adsorbates. Calcium adsorption from CaCl2 and CaSO4 was nearly linearly dependent on the equilibrium Ca2+ concentration, and was most successfully fitted to a Freundlich equation. Conversely, sulfate adsorption from K2SO4 and CaSO4 was curvilinearly dependent on equilibrium SO2‐4 concentration, conforming more closely to Langmuir adsorption behavior. Calcium adsorption was explained by nonspecific electrostatic attraction to soil clays, and did not appear to be adsorbed to any significant degree by the native organic matter. Sulfate adsorption was attributed at least in part to a ligand exchange mechanism, resulting in a measured increase in the negative charge of the soil surfaces. Simultaneous adsorption of Ca2+ and SO2‐4 from CaSO4 solutions caused an enhancement in retention of both ions at higher concentrations, despite undersaturation with respect to gypsum precipitation. A mechanism of CaSO04 ion pair adsorption on mineral surfaces is proposed in which the presence of one ion facilitates adsorption of the other.