Understanding the cation specific effects on the aqueous solubility of amino acids: from mono to polyvalent cations

Tomé, Luciana I.N.; Sousa, C.S.R.; Gomes, José R. B.; Ferreira, Olga; Coutinho, João A. P.; Pinho, Simão P.

doi:10.1039/c5ra00501a

Cited by 9 publications

(14 citation statements)

References 65 publications

(132 reference statements)

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“…The force field choice is of utmost importance to study thermodynamic properties through computer simulations. Previously, the OPLS force field was found to provide good results for aqueous-saline solutions of different amino acids systems [4,5,19]. Despite some small differences found in the absolute degrees of binding when considering different non-polarizable force fields, the relative changes along the Hofmeister series remained unchanged [19].…”

Section: Methodsmentioning

confidence: 99%

“…The remarkable impact of the salts containing divalent cations on the increase of diglycine solubility should be here highlighted. The data for alanine were taken from the literature [1,4,5,33].…”

Section: Experimental Solubility Datamentioning

confidence: 99%

“…The effect of the strongly hydrated divalent cations Mg 2+ or Ca 2+ on the solubility of different amino acids (alanine, valine and isoleucine) was studied before [4,5]. MD studies suggested that those cations do not establish important (direct) interactions with the hydrophobic parts of the amino acids, but, due to their high charge density, they were able to form charged complexes with the biomolecules, which are very soluble, promoting thus strong increases of their aqueous solubilities [4,5]. As expected, a similar behaviour for diglycine is observed mainly due to the preferential zwitterionic form of the biomolecule at the pH of the experiments.…”

Section: Experimental Solubility Datamentioning

confidence: 99%

“…A few studies have been published in this area, most focusing on model compounds such as amino acids and derivatives. In that context, we have studied the solubility of several amino acids in aqueous solutions containing inorganic salts [1][2][3][4][5]. For peptides, this type of experimental data is much scarcer.…”

Section: Introductionmentioning

confidence: 99%

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The cation effect on the solubility of glycylglycine and N-acetylglycine in aqueous solution: Experimental and molecular dynamics studies

Pérez‐Sánchez

Santos

Ferreira

et al. 2020

Journal of Molecular Liquids

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The specific interactions of ions with biomolecules in aqueous solutions play a very important role in the life sciences and biotechnology. This work aims to study the effect of NaCl, KCl, NH 4 Cl, CaCl 2 or MgCl 2 on the solubility of two glycine derivatives, glycylglycine (a.k.a. diglycine) and N-acetylglycine, and to understand the nature of the interactions present on these systems. Experimentally, upon increasing the concentration of the salts, the solubility of N-acetylglycine decreased while the solubility of diglycine increased, with divalent cations inducing a greater salting-in on the solubility of diglycine than monovalent cations. For diglycine, the results from molecular dynamics simulations correlate well with the salting-in effect with interactions involving the cation and the carboxylate group, while for neutral N-acetylglycine the interactions between the chloride anion and the hydrogen atom of the carboxylic acid group, and between the carbonyl group of the peptide bond and the cation, can be exploited to describe the generalized salting-out effect.

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Section: Methodsmentioning

confidence: 99%

Section: Experimental Solubility Datamentioning

confidence: 99%

Section: Experimental Solubility Datamentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

The cation effect on the solubility of glycylglycine and N-acetylglycine in aqueous solution: Experimental and molecular dynamics studies

Pérez‐Sánchez

Santos

Ferreira

et al. 2020

Journal of Molecular Liquids

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“…The vast difference in the crosslinking and bundling concentrations suggest that Zn 2+ and Ca 2+ interactions with vimentin are not purely electrostatic in nature. This result is reminiscent of the Hofmeister series, in which ion species are ordered according to their ability to interact with proteins, a property that still cannot be explained from first principles (17,36). The Hofmeister effect is thought to be a complex balance of the many potential interactions in the system, including ion-counterion, ion-solvent, and ion-protein interactions, which necessarily depend on intrinsic properties of the ion beyond just its charge.…”

Section: Ionic Properties Affect Interactions Within Vif Networkmentioning

confidence: 99%

Effect of the divalent cations zinc and calcium on the structure and mechanics of reconstituted vimentin intermediate filaments

Shen

Wang

et al. 2019

Preprint

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Divalent cations in a concentration-dependent manner behave as effective crosslinkers of intermediate filaments (IFs) such as vimentin IF (VIF). These interactions have been mostly attributed to their multivalency. However, ion-protein interactions often depend on the ion species, and these effects have not been widely studied in IFs. Here we investigate the effects of two biologically important divalent cations, Zn 2+ and Ca 2+ , on VIF network structure and mechanics in vitro. We find that the network structure is unperturbed at micromolar Zn 2+ concentrations, but strong bundle formation is observed at a concentration of 100 µM.Microrheological measurements show that network stiffness increases with cation concentration.However, bundling of filaments softens the network. This trend also holds for VIF networks formed in the presence of Ca 2+ , but remarkably, a concentration of Ca 2+ that is two orders higher is needed to achieve the same effect as with Zn 2+ , which suggests the importance of salt-protein interactions as described by the Hofmeister effect. Furthermore, we find evidence of competitive binding between the two divalent ion species. Hence, specific interactions between VIFs and divalent cations are likely to be an important mechanism by which cells can control their cytoplasmic mechanics. SignificanceIntermediate filaments are key structural elements within cells; they are known to form networks that can be crosslinked by divalent cations, but the interactions between the ions and the filaments are not well understood. By measuring the effects that two divalent cations, zinc and calcium, have on the structure and mechanics of vimentin intermediate filaments (VIFs), we show that although both have concentration-dependent effects on VIFs, much more calcium is needed to achieve the same effect as a small amount of zinc. Furthermore, when mixtures of the ions are present, the results suggest that there is binding competition. Thus, cells may use the presence of different cation species to precisely control their internal mechanical properties.

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Effect of Divalent Cations on the Structure and Mechanics of Vimentin Intermediate Filaments

Shen

Wang

et al. 2020

Biophysical Journal

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Divalent cations behave as effective cross-linkers of intermediate filaments (IFs) such as vimentin IF (VIF). These interactions have been mostly attributed to their multivalency. However, ion-protein interactions often depend on the ion species, and these effects have not been widely studied in IFs. Here, we investigate the effects of two biologically important divalent cations, Zn 2þ and Ca 2þ , on VIF network structure and mechanics in vitro. We find that the network structure is unperturbed at micromolar Zn 2þ concentrations, but strong bundle formation is observed at a concentration of 100 mM. Microrheological measurements show that network stiffness increases with cation concentration. However, bundling of filaments softens the network. This trend also holds for VIF networks formed in the presence of Ca 2þ , but remarkably, a concentration of Ca 2þ that is two orders higher is needed to achieve the same effect as with Zn 2þ , which suggests the importance of salt-protein interactions as described by the Hofmeister effect. Furthermore, we find evidence of competitive binding between the two divalent ion species. Hence, specific interactions between VIFs and divalent cations are likely to be an important mechanism by which cells can control their cytoplasmic mechanics.

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Understanding the cation specific effects on the aqueous solubility of amino acids: from mono to polyvalent cations

Abstract: Based on solubility and molecular dynamics studies, a consistent and refined molecular description of the effect of the cation on the solubility of amino acids based on specific interactions of the cations with the negatively charged moieties of the biomolecules is proposed.

Cited by 9 publications

References 65 publications

The cation effect on the solubility of glycylglycine and N-acetylglycine in aqueous solution: Experimental and molecular dynamics studies

The cation effect on the solubility of glycylglycine and N-acetylglycine in aqueous solution: Experimental and molecular dynamics studies

Effect of the divalent cations zinc and calcium on the structure and mechanics of reconstituted vimentin intermediate filaments

Effect of Divalent Cations on the Structure and Mechanics of Vimentin Intermediate Filaments

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