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Assembly and Characterization of Polyelectrolyte Complex Micelles
Published on: March 2, 2020
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Effects of conformational ordering on protein/polyelectrolyte electrostatic complexation: ionic binding and chain
Yiping Cao1, Yapeng Fang1,2, Katsuyoshi Nishinari1,2
1Glyn O. Phillips Hydrocolloid Research Centre, School of Food and Pharmaceutical Engineering, Faculty of Light Industry, Hubei University of Technology, Wuhan 430068, China.
Scientific Reports
|April 1, 2016
Summary
This study reveals how κ-carrageenan (κ-car) and gelatin interact, showing that ionic binding and chain stiffening influence their electrostatic complexation. Changes in κ-car conformation can either enhance or suppress complex formation.
Area of Science:
- Biochemistry
- Materials Science
- Polymer Chemistry
Background:
- Protein/polyelectrolyte interactions are crucial in biological processes and applications.
- Electrostatic complexation is influenced by conformational changes.
Purpose of the Study:
- To investigate the electrostatic complexation between κ-carrageenan (κ-car) and type B gelatin.
- To analyze the impact of κ-car conformational ordering on this complexation.
Main Methods:
- Studied κ-car/gelatin complexation under varying ionic conditions (KCl, Me4NI).
- Analyzed effects of conformational ordering (ionic binding, chain stiffening) on complexation.
Main Results:
- Ionic binding of K(+) and I(-) ions initially alters charge density and binding sites, affecting complexation.
- Chain stiffening and increased helix length in κ-car (θ > 0.30) dominate, leading to dissociation of electrostatic complexation.
- Chain stiffening effect explained by double helix association.
Conclusions:
- Conformational ordering in κ-car significantly modulates electrostatic complexation with gelatin.
- The interplay of ionic binding and chain stiffening dictates the complexation outcome.
- Findings offer insights into controlling protein/polyelectrolyte interactions.
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