Abstract

Biological macromolecules including nucleic acids, proteins, and glycosaminoglycans are typically anionic and can span domains of up to hundreds of nanometers and even micron length scales. The structures exist in crowded environments that are dominated by multivalent electrostatic interactions that can be modeled using mean-field continuum approaches that represent underlying molecular nanoscale biophysics. We develop such models for glycosaminoglycan brushes using steady state modified Poisson-Boltzmann models that incorporate important ion-specific (Hofmeister) effects. The results quantify how electroneutrality is attained through ion electrophoresis, spatially varying permittivity hydration forces, and ion-specific pairing. Brush-salt interfacial profiles of the electrostatic potential as well as bound and unbound ions are characterized for imposed jump conditions across the interface. The models should be applicable to many intrinsically disordered biophysical environments and are anticipated to provide insight into the design and development of therapeutics and drug-delivery vehicles to improve human health.

Department(s)

Business and Information Technology

Second Department

Chemical and Biochemical Engineering

Comments

Claremont Graduate University, Grant None

International Standard Serial Number (ISSN)

2470-0053; 2470-0045

Document Type

Article - Journal

Document Version

Final Version

File Type

text

Language(s)

English

Rights

© 2025 American Physical Society, All rights reserved.

Publication Date

01 Feb 2023

PubMed ID

36932500

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