Hofmeister‐Effekte unter der Lupe: Die direkte Anion‐Amid‐Bindung ist schwächer als die Kation‐Amid‐Bindung

Ion-protein interactions are important for protein function, yet challenging to rationalize due to the multitude of ion-protein interaction possibilities. To explore specific ion effects on protein binding sites, we investigate the interaction of different salts with the zwitterionic peptide triglycine in solution. Dielectric spectroscopy experiments show that salts affect the peptide's reorientational dynamics, with a more pronounced effect of denaturing cations (Li + , guanidinium Gdm + ) and anions (I -, SCN -) than weakly denaturing ones (K + , Cl -). Notably, we find the effect of Gdm + and Li + to be comparable. Molecular dynamics simulations confirm the enhanced binding of Gdm + and Li + to triglycine, yet with a different binding geometry: While Li + predominantly binds to the C-terminal carboxylate group, bidentate binding to the terminus and the nearest amide is particularly important for Gdm + . This bidentate binding markedly affects peptide conformation. As such, this bidentate binding geometry may help explain the high denaturation activity of Gdm + salts.Specific ion effects, i.e., salts affecting macroscopic properties like surface tension, [1] solubilities, [2,3] interfacial potentials, [4] colloidal stability, [5] and biological activity [5,6] are ubiquitous. Yet, a molecular-level understanding of how ions alter such properties beyond electrostatic effects has not been fully obtained. [7] In particular, understanding how ions affect proteins remains challenging. [6,8,9] Such challenges arise from the structural complexity of proteins and the concomitant broad range of chemically different molecular protein sites. [10] Model systems such as amide-rich molecules have been often used to elucidate ionprotein interaction. [3,[11][12][13][14][15][16][17][18] These amide models, however, lack charged residues (e.g., the C-and N-termini) that are intrinsically sensitive to electrostatic interaction with

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Spezifische Ionen‐Effekte am Beispiel eines Oligopeptids: die Rolle zweizähniger Koordination beim Guanidinium‐Kation

Balos

Marekha

Malm

et al. 2018

Angewandte Chemie

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Specific Ion Effects on an Oligopeptide: Bidentate Binding Matters for the Guanidinium Cation

et al. 2018

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Ion–protein interactions are important for protein function, yet challenging to rationalize owing to the multitude of possible ion–protein interactions. To explore specific ion effects on protein binding sites, we investigate the interaction of different salts with the zwitterionic peptide triglycine in solution. Dielectric spectroscopy shows that salts affect the peptide's reorientational dynamics, with a more pronounced effect for denaturing cations (Li+, guanidinium (Gdm+)) and anions (I−, SCN−) than for weakly denaturing ones (K+, Cl−). The effects of Gdm+ and Li+ were found to be comparable. Molecular dynamics simulations confirm the enhanced binding of Gdm+ and Li+ to triglycine, yet with a different binding geometry: While Li+ predominantly binds to the C‐terminal carboxylate group, bidentate binding to the terminus and the nearest amide is particularly important for Gdm+. This bidentate binding markedly affects peptide conformation, and may help to explain the high denaturation activity of Gdm+ salts.

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Hofmeister Series: From Aqueous Solution of Biomolecules to Single Cells and Nanovesicles

Ewing

2023

ChemBioChem

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Hofmeister effects play a critical role in numerous physicochemical and biological phenomena, including the solubility and/or accumulation of proteins, the activities of enzymes, ion transport in biochannels, the structure of lipid bilayers, and the dynamics of vesicle opening and exocytosis. This minireview focuses on how ionic specificity affects the physicochemical properties of biomolecules to regulate cellular exocytosis, vesicular content, and nanovesicle opening. We summarize recent progress in further understanding Hofmeister effects on biomacromolecules and their applications in biological systems. These important steps have increased our understanding of the Hofmeister effects on cellular exocytosis, vesicular content, and nanovesicle opening. Increasing evidence is firmly establishing that the ions along the Hofmeister series play an important role in living organisms that has often been ignored.

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Hofmeister‐Effekte unter der Lupe: Die direkte Anion‐Amid‐Bindung ist schwächer als die Kation‐Amid‐Bindung

Cited by 5 publications

References 42 publications

Spezifische Ionen‐Effekte am Beispiel eines Oligopeptids: die Rolle zweizähniger Koordination beim Guanidinium‐Kation

Spezifische Ionen‐Effekte am Beispiel eines Oligopeptids: die Rolle zweizähniger Koordination beim Guanidinium‐Kation

Specific Ion Effects on an Oligopeptide: Bidentate Binding Matters for the Guanidinium Cation

Hofmeister Series: From Aqueous Solution of Biomolecules to Single Cells and Nanovesicles

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