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Salt-Added Solutions of Markov Polyampholytes: Diagram of States, Antipolyelectrolyte Effect, and Self-Coacervate Dynamics

Cite this: Macromolecules 2023, 56, 13, 5201–5216
Publication Date (Web):June 16, 2023
https://doi.org/10.1021/acs.macromol.3c00512
Copyright © 2023 American Chemical Society

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    Abstract

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    Field-theoretic and scaling approaches are combined to predict conformational behaviors of single-chain globally neutral polyampholytes (PAs) in the presence of salt, the viscosity of their dilute solutions, and the rheology of condensed self-coacervate phases. To reveal the role of the monomer sequence, we consider PAs with Markov statistics of positive and negative charges. The diagram of globular regimes of single-chain PAs in Θ solvent is constructed with the coordinates of the charge blockiness and salt concentrations. For highly flexible chains, it contains six scaling regimes corresponding to low/high salt concentrations and (i) almost alternating, (ii) random correlated, and (iii) highly blocky sequences of ionic monomers. At increasing salt concentration, PAs of any sequence swell until reaching an ideal-coil size. The amplitude of the salt-induced globule-to-coil transition increases with increasing charge blockiness. So does the change in the viscosity of dilute PA solutions, indicating the sequence specificity in the antipolyelectrolyte effect. The similarity between the internal structure of the globules and macroscopic self-coacervate phases enables prediction of the viscosity of the latter. The respective scaling dependencies for self-coacervates of short unentangled and long entangled PAs are provided. Self-coacervate viscosity is the highest for the most blocky PAs and, for any sequence, decreases with the addition of salt. Our findings serve as important guidelines for understanding the dynamics of intracellular condensates, which form from polyampholytic disordered proteins/regions and exhibit the salt-induced viscosity drop described herein.

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    The Supporting Information is available free of charge at https://pubs.acs.org/doi/10.1021/acs.macromol.3c00512.

    • (I) Decomposing the RPA Coulomb and Edwards corrections; (II) applicability range of the RPA; (III) surface tension of polyampholyte globules and self-coacervates (PDF)

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    Cited By

    This article is cited by 1 publications.

    1. Artem M. Rumyantsev, Alexey A. Gavrilov, Albert Johner. Complete Diagram of Conformational Regimes for Polyampholytic Disordered Proteins. Macromolecules 2024, 57 (11) , 5533-5544. https://doi.org/10.1021/acs.macromol.4c00429