ArticleBiomacromolecules2024
Effects of Ionic Strength on the Morphology, Scattering, and Mechanical Response of Neurofilament-Derived Protein Brushes.
Article in Biomacromolecules, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed.
- Dissecting neurofilament tail sequence-phosphorylation-structure relationships with multicomponent reconstituted protein brushes.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Neurofilament Biophysics: From Structure to Biomechanics.Molecular biology of the cell · 2024Review
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Authors and funding
5 authors.
Funding
Abstract
Protein brushes not only play a key role in the functionality of neurofilaments but also have wide applications in biomedical materials. Here, we investigate the effect of ionic strength on the morphology of protein brushes using continuous-space self-consistent field theory. A coarse-grained multiblock charged macromolecular model is developed to capture the chemical identity of amino acid sequences. For neurofilament heavy (NFH) brushes at pH 2.4, we predict three morphological regimes: swollen brushes, condensed brushes, and coexisting brushes, which consist of both a dense inner layer and a diffuse outer layer. The brush height predicted by our theory is in good agreement with the experimental data for a wide range of ionic strengths. The dramatic height decrease is a result of the electrostatic screening-induced transition from the overlapping state to the isolated state of the coexisting brushes. We also studied the evolution of the scattering and mechanical responses accompanying the morphological change. The oscillation in the reflectivity spectra characterizes the existence and microstructure of the inner condensed layer, whereas the shoulder in the force spectra signifies a swollen morphology.
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