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Electrostatic polyelectrolyte-myoglobin complexes: relaxation dynamics and viscosity under hydrated and aqueous
Achilleas Pipertzis1, Angeliki Chroni2, Andrzej Marcinkowski3
1Department of Physics and Astronomy, Chalmers University of Technology, 41296, Gothenburg, Sweden. achilleas.pipertzis@chalmers.se.
Soft Matter
|July 29, 2026
Summary
This study reveals how synthetic polyelectrolytes and myoglobin form nanoscale complexes, increasing viscosity and the copolymer
Area of Science:
- Polymer science
- Biophysics
- Materials science
Background:
- Understanding polyelectrolyte-protein interactions is crucial for biomaterials and drug delivery.
- Synthetic polyelectrolytes offer tunable properties for complex formation.
- Myoglobin serves as a model globular protein for studying electrostatic interactions.
Purpose of the Study:
- To investigate the structural characteristics of polyelectrolyte-protein electrostatic complexes.
- To determine the impact of complex formation on molecular relaxation dynamics and viscosity.
- To elucidate the structure-dynamics-property relationships in these systems.
Main Methods:
- Atomic Force Microscopy (AFM) for nanoscale imaging.
- X-ray scattering techniques for structural analysis.
- Rheological and ball viscometry measurements for viscosity determination.
Main Results:
- Formation of nanoscale core-shell assemblies (approx. 50 nm) and larger aggregates (200-250 nm).
- Strong electrostatic interactions significantly slow copolymer dynamics and increase glass transition temperature (Tg) by ~15 K.
- Macroscopic viscosity increases due to complex formation and aggregation.
Conclusions:
- Demonstrates the formation of distinct nanoscale structures between a synthetic polyelectrolyte and myoglobin.
- Highlights the significant influence of electrostatic interactions on polymer dynamics and material properties.
- Provides fundamental insights into polyelectrolyte-protein complex behavior for advanced material design.
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