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At least 109 records · Page 6Linked to original sources
PubMed2005

Kinetics and functional studies on interaction between the replicase proteins of Tomato Bushy Stunt Virus: requirement of p33:p92 interaction for replicase assembly.

The assembly of the functional replicase complex via protein:protein and RNA:protein interactions among the viral-coded proteins, host factors and the viral RNA on cellular membranes is a key step in the replication process of plus-stranded RNA viruses. In this work, we have characterized essential interactions between p33:p33 and p33:p92 replication proteins of Tomato bushy stunt virus (TBSV), a tombusvirus with a non-segmented, plus-stranded RNA genome. Surface plasmon resonance (SPR) measurements with purified recombinant p33 and p92 demonstrate that p33 interacts with p92 in vitro and that the interaction requires the S1 subdomain, whereas the S2 subdomain plays lesser function. Kinetic SPR analyses showed that binding of S1 subdomain to the C-terminal half of p33 takes place with moderate binding affinity in the nanomolar range whereas S2 subdomain binds to p33 with micromolar affinity. Using mutated p33 and p92 proteins, we identified critical amino acid residues within the p33:p92 interaction domain that play essential role in replication and the assembly of the tombusviral replicase. In addition, we show that interaction takes place between replication proteins of TBSV and the closely related Cucumber necrosis virus but not between TBSV and the more distantly related Turnip crinkle virus, suggesting that selective protein interactions might prevent the assembly of chimeric replicases carrying replication proteins from different viruses during mixed infections.

Amino Acid Substitution↗
PubMed2006

Grapefruit-drug interactions: can interactions with drugs be avoided?

Grapefruit is rich in flavonoids, which have been demonstrated to have a preventive influence on many chronic diseases, such as cancer and cardiovascular disease. However, since the early 1990s, the potential health benefits of grapefruit have been overshadowed by the possible risk of interactions between drugs and grapefruit and grapefruit juice. Several drugs interacting with grapefruit are known in different drug classes, such as HMG-CoA reductase inhibitors, calcium antagonists, and immunosuppressives. Currently known mechanisms of interaction include the inhibition of cytochrome P450 as a major mechanism, but potential interactions with P-glycoprotein and organic anion transporters have also been reported. This review is designed to provide a comprehensive summary of underlying mechanisms of interaction and human clinical trials performed in the area of grapefruit drug interactions and to point out possible replacements for drugs with a high potential for interactions.

Citrus paradisi↗
PubMed1999

Adverse drug interactions in dental practice: interactions associated with analgesics, Part III in a series.

BACKGROUND: Numerous reports of drug interactions exist, yet not all are valid in or pertinent to dentistry. This article provides an overview of drug interactions with analgesics and identifies those that are clinically relevant. METHODS: The author reviewed reports of drug interactions involving nonsteroidal anti-inflammatory drugs, or NSAIDs (including aspirin), acetaminophen and opioids to determine the interactions' validity and clinical relevance. Consistent with the practice followed in other articles in this series, the author determined the significance of the proposed interaction by gauging its reported severity and the quality of the documentation. RESULTS AND CONCLUSIONS: NSAIDs should not be taken by patients taking high-dose methotrexate, anticoagulants or alcohol. They should be avoided in elderly or renally impaired patients taking digoxin, and avoided over the long term in those taking other NSAIDs. It is possible that NSAIDs should not be given to patients taking lithium, but future studies should be conducted to confirm this. Use of NSAIDs likely is appropriate in the short term with patients taking antihypertensives, unless they have severe congestive heart disease. Aspirin should not be given to patients taking oral hypoglycemics, valproic acid or carbonic anhydrase inhibitors. Acetaminophen may be given in the short term to any patient with a healthy liver, but it should not be given to a patient who has stopped drinking alcohol after chronic intake. Opioids should not be combined with alcohol, and meperidine must be avoided in the patient who has taken monoamine oxidase inhibitors in the previous 14 days. CLINICAL IMPLICATIONS: Drug interactions with analgesics are often reported, but only a small number have clinical relevance in dentistry. Awareness of the significance of these interactions will allow dentists to prescribe analgesics optimally and minimize the potential for adverse reactions.

Acetaminophen↗
PubMed1998

[Role of food interaction pharmacokinetic studies in drug development. Food interaction studies of theophylline and nifedipine retard and buspirone tablets].

Due to several mechanism, meals may modify the pharmacokinetics of drug products, thereby eliciting to clinically significant food interaction. Food interactions with the drug substance and with the drug formulation should be distinguished. Food interaction of different drug products containing the same active ingredient can be various depending on the pharmaceutical formulation technology. Particularly, in the case of modified release products, the food/formulation interaction can play an important role in the development of food interaction. Well known example, that bioavailability of theophylline can be influenced in different way (either increased, decreased or unchanged) by concomitant intake of food in the case of different sustained release products. The role and methods of food interaction studies in the different kinds of drug development (new chemical entity, modified release products, generics) are reviewed. Prediction of food effect response on the basis of the physicochemical and pharmacokinetic characteristics of the drug molecule or formulations is discussed. The results of three food interaction studies carried out the products of EGIS Pharmaceuticals Ltd. are also reviewed. The pharmacokinetic parameters of theophyllin 400 mg retard tablet were practically the same in both fasting condition and administration after consumption of a high fat containing standard breakfast. The ingestion of a high fat containing breakfast, increased the AUC of nifedipine from 259.0 +/- 101.2 ng h/ml to 326.7 +/- 122.5 ng h/ml and Cmax from 34.5 +/- 15.9 ng/ml to 74.3 +/- 23.9 ng/ml in case of nifedipine 20 mg retard tablet, in agreement with the data of literature. The statistical evaluation indicated significant differences between the pharmacokinetic parameters in the case of two administrations (before and after meal). The effect of a high fat containing breakfast for a generic version of buspiron 10 mg tablet and the bioequivalence after food consumption were studied in a single-dose, three-way (test and reference products administered after consumption of standard breakfast, as well as test product in fasting condition), cross-over, food effect bioequivalence study. According to the results, the test product--which, in a former study proved to be bioequivalent with the reference product in fasting state--is bioequivalent with the reference product under feeding conditions and the food intake influenced the pharmacokinetics of the test tablets.

Buspirone↗
PubMed2000

Metal ligand aromatic cation-pi interactions in metalloproteins: ligands coordinated to metal interact with aromatic residues.

Cation-pi interactions between aromatic residues and cationic amino groups in side chains and have been recognized as noncovalent bonding interactions relevant for molecular recognition and for stabilization and definition of the native structure of proteins. We propose a novel type of cation-pi interaction in metalloproteins; namely interaction between ligands coordinated to a metal cation--which gain positive charge from the metal--and aromatic groups in amino acid side chains. Investigation of crystal structures of metalloproteins in the Protein Data Bank (PDB) has revealed that there exist quite a number of metalloproteins in which aromatic rings of phenylalanine, tyrosine, and tryptophan are situated close to a metal center interacting with coordinated ligands. Among these ligands are amino acids such as asparagine, aspartate, glutamate, histidine, and threonine, but also water and substrates like ethanol. These interactions play a role in the stability and conformation of metalloproteins, and in some cases may also be directly involved in the mechanism of enzymatic reactions, which occur at the metal center. For the enzyme superoxide dismutase, we used quantum chemical computation to calculate that Trp163 has an interaction energy of 10.09 kcal mol(-1) with the ligands coordinated to iron.

Alcohol Dehydrogenase↗
PubMed2003

Improved sensitivity of biomolecular interaction analysis mass spectrometry for the identification of interacting molecules.

Biological functions of most macromolecules depend on their ability to interact with other molecules and a great challenge is the complete description of the protein interaction networks. Biomolecular interaction analysis (BIA) is an optical technology that uses the surface plasmon resonance phenomenon for characterizing macromolecular interactions between an analyte in solution and its ligand immobilized on a sensor chip. Further identification of interacting proteins can be achieved by combining this nondestructive method to mass spectrometry (MS). The BIA-MS approach represents a promising tool in proteomics for the characterization of protein/protein interactions. In this study, we report on the improved sensitivity in the identification of an unknown protein bound to a known ligand by a rapid and simple BIA-MS approach. We took advantage of a new automatic and very reproducible microelution procedure available on BIACORE 3000 instruments, called "microrecovery", to elute the bound protein from the sensor chip. Protein identification was then achieved after tryptic digestion by matrix-assisted laser desorption/ionization-time of flight mass mapping and database search. The strategy was succesfully applied to the model protein SHP2 tyrosine phosphatase interacting with an immunoreceptor tyrosine-based inhibitory motif sequence of the sst2 somatostatin receptor. Optimization of the BIA-MS approach allowed the unambiguous identification of 10-20 fmol of the protein specifically trapped from a complex mixture of cytosolic extracts.

Amino Acid Sequence↗
PubMed1990

Supportive interactions, negative interactions, and depressed mood.

Research on the association between social relationships and emotional functioning has emphasized the health-promoting effects of social support. Yet there is reason to believe that the absence of negative social interactions may be more important for mental health than the presence of supportive interactions. In this investigation we clarify important characteristics concerning the source, the recipient, and the combined influence of support and negativity. Data are presented regarding supportive and negative interactions with spouse, relatives, and friends; regression analyses suggest that negative interactions are more predictive of depressed mood than supportive interactions (specifically with spouse and friends). We also document several specifications suggesting directions for future research on the special importance of interactions in intimate relationships and the synergistic effects of situations in which supportive and negative interactions both occur.

Adaptation, Psychological↗
PubMed1979

Interaction of purple membrane with solvents. II. Mode of interaction.

Using the solubility parameter mapping technique (Eisenbach, M., Caplan, S.R. and Tanny, G (1979) Biochim. Biophys. Acta 554, 269-280) we studied spectroscopically the mode of interaction between the purple membrane of Halobacterium halobium and pure organic solvents or solvent mixtures. Although the interacting solvents formed a well-defined closed region in the interaction maps, mapping the modes of interaction did not reveal a closed region for each spectrally classifiable type. A suggested interpretation for this is that interaction with the purple membrane chromophore requires that a solvent (or solvent mixture) possess apolar groups in order to obtain access to the chromophore, together with a polar character and hydrogen-bonding capacity. The mode of interaction, however, is dependent on the specificity of the reactive group of the solvent for retinal, and this has nothing to do with membrane properties. We also examined the influence of the duration of the interaction and of illumination. Some solvents appeared to react more sluggishly than others, but no generalization in terms of the solubility parameter mapping was found, probably because the map describes thermodynamic rather than kinetic phenomena. The only effect of illumination was to enhance the reaction of some of these solvents. It did not change the solubility parameters of purple membrane.

Bacteriorhodopsins↗
PubMed1978

Nucleic acid interaction with VERO cells. A temperature barrier in the interaction pattern.

The interaction of VERO cell monolayers with spin (nitroxide)-(labeled polynucleotides (1(N)n) was examined by electron spin resonance (ESR) spectroscopy at various temperatures. Nitroxide labels covalently linked to (A)n, (dUfl)n, (U)n and (A)n . (U)n were used to monitor the interaction. The VERO cells were grown on small quartz plates with a cell viability of 95% or better and then used directly for the ESR studies. The ESR results indicated that the interaction between VERO cells and spin-labeled nucleic acids is temperature dependent. No temperature dependence was found when VERO cells were in contact with nitroxide radicals which were free in solution or covalently bound to Sepharose 4B. The temperature dependence established with nitroxide-labeled nucleic acids indicates that a temperature barrier must exist between 20 and 26 degrees C for the interaction between nucleic acids and VERO cells; namely, at 26 degrees C or above spin-labeled nucleic acids interact significantly with a VERO cell surface; whereas, at 20 degrees C the ESR signal reports no interaction. It is concluded that a temperature-dependent phase transition of membrane components or cell surface products active at 26 degrees C or above play a key role in the nucleic acid cell surface interaction process.

Cell Line↗
PubMed1985

Nonimmune lymphocyte-macrophage interaction. II. Evidence that the interaction involves sulfated polysaccharide recognition.

This paper describes attempts to determine the molecular basis of the nonimmune interaction between lymphocytes and macrophages. Initial studies revealed that the interaction could be inhibited by simple sugars, six out of the thirty-five tested being inhibitory. Furthermore, the majority of the inhibitory sugars were charged and subsequent studies revealed that some sulfated polysaccharides, notably kappa-carrageenan, were potent inhibitors of the interaction. Further experiments revealed that the lymphocyte-macrophage interaction was indeed mediated by kappa-carrageenan-specific receptors on lymphocytes. The results supporting such a conclusion were as follows: When the interacting cells were preincubated with kappa-carrageenan, it was found that kappa-carrageenan exerted its inhibitory effect at the lymphocyte rather than the macrophage level. Separation of splenocytes into kappa-carrageenan-binding and -nonbinding subpopulations resulted in a corresponding enrichment and depletion of lymphocytes that reacted with macrophages. Lymphocytes were found to express kappa-carrageenan-reactive molecules, these molecules being detected on the surface of lymphocytes by rosetting and in detergent lysates as hemagglutinins. Furthermore, the polyanion specificity of these kappa-carrageenan-specific receptors/hemagglutinins closely resembled the specificity of inhibition of the lymphocyte-macrophage interaction. Pronase-resistant material in macrophage, but not lymphocyte lysates, effectively inhibited both the lymphocyte-macrophage interaction and the recognition of kappa-carrageenan by lymphocytes, suggesting that a kappa-carrageenan-like structure is expressed by macrophages.

Animals↗
PubMed2006

Evidence for the interaction of the regulatory protein Ki-1/57 with p53 and its interacting proteins.

Ki-1/57 is a cytoplasmic and nuclear phospho-protein of 57 kDa and interacts with the adaptor protein RACK1, the transcription factor MEF2C, and the chromatin remodeling factor CHD3, suggesting that it might be involved in the regulation of transcription. Here, we describe yeast two-hybrid studies that identified a total of 11 proteins interacting with Ki-1/57, all of which interact or are functionally associated with p53 or other members of the p53 family of proteins. We further found that Ki-1/57 is able to interact with p53 itself in the yeast two-hybrid system when the interaction was tested directly. This interaction could be confirmed by pull down assays with purified proteins in vitro and by reciprocal co-immunoprecipitation assays from the human Hodgkin analogous lymphoma cell line L540. Furthermore, we found that the phosphorylation of p53 by PKC abolishes its interaction with Ki-1/57 in vitro.

Animals↗
PubMed2006

RGSZ1 interacts with protein kinase C interacting protein PKCI-1 and modulates mu opioid receptor signaling.

Protein kinase C interacting protein (PKCI-1) was identified among the potential interactors from a yeast two hybrid screen of human brain library using N terminal of RGSZ1 as a bait. The cysteine string region, unique to the RZ subfamily, contributes to the observed interaction because PKCI-1 interacted with N-terminus of RGS17 and GAIP, but not with that of RGS2 or RGS7 where cysteine string motif is absent. The interaction between RGSZ1 and PKCI-1 was confirmed by coimmunoprecipitation and immunofluorescence. PKCI-1 and RGSZ1 could be detected by coimmunoprecipitation using 14-3-3 antibody in cells transfected with PKCI-1 or RGSZ1 respectively, but when transfected with PKCI-1 and RGSZ1 together, only RGSZ1 could be detected. Phosphorylation of Galphaz by protein kinase C (PKC) reduces the ability of the RGS to effectively function as GTPase accelerating protein for Galphaz, and interferes with ability of Galphaz to interact with betagamma complex. We investigated the roles of 14-3-3 and PKCI-1 in phosphorylation of Galphaz. Phosphorylation of Galphaz by PKC was inhibited by 14-3-3 and the presence of PKCI-1 did not provide any further inhibition. PKCI-1 interacts with mu opioid receptor and suppresses receptor desensitization and PKC related mu opioid receptor phosphorylation [W. Guang, H. Wang, T. Su, I.B. Weinstein, J.B. Wang, Mol. Pharmacol. 66 (2004) 1285.]. Previous studies have also shown that mu opioid receptor co-precipitates with RGSZ1 and influence mu receptor signaling by acting as effector antagonists [J. Garzon, M. Rodriguez-Munoz, P. Sanchez-Blazquez, Neuropharmacology 48 (2005) 853., J. Garzon, M. Rodriguez-Munoz, A. Lopez-Fando, P. Sanchez-Blazquez Neuropsychopharmacology 30 (2005) 1632.]. Inhibition of cAMP by mu opioid receptor was significantly reduced by RGSZ1 and this effect was enhanced in combination with PKCI-1. Our studies thus provide a link between the previous observations mentioned above and indicate that the major function of PKCI-1 is to modulate mu opioid receptor signaling pathway along with RGSZ1, rather than directly mediating the Galphaz RGSZ1 interaction.

14-3-3 Proteins↗
PubMed2004

Thermodynamics and kinetics of non-native interactions in protein folding: a single point mutant significantly stabilizes the N-terminal domain of L9 by modulating non-native interactions in the denatured state.

Comparatively little is known about the role of non-native interactions in protein folding and their role in both folding and stability is controversial. We demonstrate that non-native electrostatic interactions involving specific residues in the denatured state can have a significant effect upon protein stability and can persist in the transition state for folding. Mutation of a single surface exposed residue, Lys12 to Met, in the N-terminal domain of the ribosomal protein L9 (NTL9), significantly increased the stability of the protein and led to faster folding. Structural and energetic studies of the wild-type and K12M mutant show that the 1.9 kcal mol(-1) increase in stability is not due to native state effects, but rather is caused by modulation of specific non-native electrostatic interactions in the denatured state. pH dependent stability measurements confirm that the increased stability of the K12M is due to the elimination of favorable non-native interactions in the denatured state. Kinetic studies show that the non-native electrostatic interactions involving K12 persist in the transition state. The analysis demonstrates that canonical Phi-values can arise from the disruption of non-native interactions as well as from the development of native interactions.

Lysine↗
PubMed2006

Specific interaction of CXCR4 with CD4 and CD8alpha: functional analysis of the CD4/CXCR4 interaction in the context of HIV-1 envelope glycoprotein-mediated membrane fusion.

We investigated possible interactions between HIV-1 receptor (CD4) and the main coreceptors CXCR4 and CCR5. We found that CD4 and CXCR4 coexpressed in 293T cells form a complex that can be immunoprecipitated with antibodies directed against the extracellular domain of either protein. Mutagenesis revealed that the CD4/CXCR4 interaction maps to two previously uncharacterized basic motifs in the cytoplasmic domain of CD4. HIV-1 envelope glycoprotein-mediated membrane fusion was found to be independent of the ability of CD4 and CXCR4 to interact, whether fusion was studied in a virus-cell or a cell-cell model. However, this interaction might explain the adaptation of HIV-1 to CXCR4 as an alternative to CCR5. We found that CXCR4 also interacts with the cytoplasmic domain of CD8alpha in a way that is similar to the CD4/CXCR4 interaction. The CD4/CXCR4 and CD8alpha/CXCR4 interactions may thus be involved in cellular signaling pathways shared by the CD4 and CD8alpha molecules.

CD4 Antigens↗
PubMed2001

PLS modeling of chimeric MS04/MSH-peptide and MC1/MC3-receptor interactions reveals a novel method for the analysis of ligand-receptor interactions.

A novel method has been developed for the analysis of ligand-receptor interactions. The method utilizes binding data generated from the analysis of chimeric proteins with chimeric peptides. To each chimeric part of the peptide and receptor are assigned descriptors, thus creating a matrix of X descriptors. These descriptors are then correlated with the experimentally determined interaction binding affinities for each chimeric receptor/peptide pair by use of partial least-squares projection to latent structures (PLS). The method was applied to analyze the interactions of chimeric MSH-peptides with wild-type MC1 and MC3 receptors, and MC1/MC3 receptor chimeras (in total 40 peptide-receptor combinations). Two types of PLS models could be created, one that revealed the relationships between receptor and peptide structure and peptide binding pK(i) values (i.e., affinity) (R2 and Q2 being 0.71 and 0.62, respectively), and another that revealed the relationships between peptide and receptor structure and peptide-receptor selectivity (R2 and Q2 being 0.64 and 0.57, respectively). After addition of cross-terms these models improved significantly; the R2 and Q2 being 0.93 and 0.75 for affinity, and 0.92 and 0.72 for selectivity, respectively. The analysis shows that the high affinity of the MSH-peptides is primarily achieved by interactions of the peptides' C-terminal amino acids with TM2 and TM3 of the receptor, and, to a lesser extent, by the interaction of the N-terminus with TM1, TM2 and TM3 of the receptor. However, in contrast, the MC1 receptor selectivity is primarily determined by an interaction of the peptides' N-termini with TM2/3 of the receptor. Moreover, the cross-terms of the PLS model revealed the existence of a strong interaction between TM6/7 and TM2/3 of the receptors.

Amino Acid Sequence↗
PubMed1993

The search for structure-specific nucleic acid-interactive drugs: effects of compound structure on RNA versus DNA interaction strength.

The RNA genomes of a number of pathogenic RNA viruses, such as HIV-1, have extensive folded conformations with imperfect A-form duplexes that are essential for virus function and could serve as targets for structure-specific antiviral drugs. As an initial step in the discovery of such drugs, the interactions with RNA of a wide variety of compounds, which are known to bind to DNA in the minor groove, by classical or by threading intercalation, have been evaluated by thermal melting and viscometric analyses. The corresponding sequence RNA and DNA polymers, poly(A).poly(U) and poly(dA).poly(dT), were used as test systems for analysis of RNA binding strength and selectivity. Compounds that bind exclusively in the minor groove in AT sequences of DNA (e.g., netropsin, distamycin, and a zinc porphyrin derivative) do not have significant interactions with RNA. Compounds that bind in the minor grove in AT sequences of DNA but have other favorable interactions in GC sequences of DNA (e.q., Hoechst 33258, DAPI, and other aromatic diamidines) can have very strong RNA interactions. A group of classical intercalators and a group of intercalators with unfused aromatic ring systems contain compounds that intercalate and have strong interactions with RNA. At this time, no clear pattern of molecular structure that favors RNA over DNA interactions for intercalators has emerged. Compounds that bind to DNA by threading intercalation generally bind to RNA by the same mode, but none of the threading intercalators tested to date have shown selective interactions with RNA.

DNA↗
PubMed2001

Olefinic vs. aromatic pi-H interaction: a theoretical investigation of the nature of interaction of first-row hydrides with ethene and benzene.

The nature and origin of the pi-H interaction in both the ethene (olefinic) and benzene (aromatic) complexes of the first-row hydrides (BH(3), CH(4), NH(3), H(2)O, and HF) has been investigated by carrying out high level ab initio calculations. The results indicate that the strength of the pi-H interaction is enhanced as one progresses from CH(4) to HF. Unlike conventional H-bonds, this enhancement cannot be simply explained by the increase in electrostatic interactions or the electronegativity of the atom bound to the pi H-bonded proton. The contributions of each of the attractive (electrostatic, inductive, dispersive) and repulsive exchange components of the total binding energy are important. Thus, the inductive energy is highly correlated to the olefinic pi-H interaction as we progress from CH(3) to HF. On the other hand, both electrostatic and inductive energies are important in the description of the aromatic pi-H interaction. In either case, the contribution of dispersion energies is vital to obtain an accurate estimate of the binding energy. We also elaborate on the correlation of various interaction energy components with changes in geometries and vibrational frequencies. The red-shift of the nu(Y-H) mode is highly correlated to the inductive interaction. The dramatic increase in the exchange repulsion energies of these pi complexes as we progress from CH(4) to HF can be correlated to the blue-shift of the highly IR active out-of-plane bending mode of the pi system.

Journal Article↗
PubMed2000

Hydrogen bonding and electrostatic interaction contributions to the interaction of a cationic drug with polyaspartic acid.

PURPOSE: To determine the mechanism and identify forces of interaction between polyaspartic acid and diminazene (a model drug). Such knowledge is essential for the design of polymeric drug delivery systems that are based on molecular self-assembly into complexes or micellar type systems. METHODS: Complex formation was studied by isothermal titration microcalorimetry and the McGhee von Hippel model was applied to obtain K(obs), deltaH(obs), and n(obs). The calorimetry data were compared with both an optical density study and the amount of free/complexed drug. RESULTS: The diminazene-polyaspartic acid interaction is enthalpically driven, whereby one diminazene molecule interacts with two monomers of polyaspartic acid. The dependence of K(obs) on salt concentration reveals a contribution of electrostatic interactions. However, applying Manning's counter ion condensation theory shows that the major driving force for the complex formation is hydrogen bonding, with interfacial water molecules remaining buried within the complex. The modelling of the pH dependence of K(obs) and deltaH(obs) demonstrates that the ionization of carboxylic groups of polyaspartic acid is a prerequisite for the interaction. CONCLUSIONS: Complex formation between diminazene and polyaspartic acid is driven by both electrostatic interactions and hydrogen bonding, with the latter being the dominating force. Although electrostatic interactions are not the major driving force, ionization of the drug and polymer is essential for complex formation.

Cations↗