Related Experiment Video
Updated: Dec 30, 2025

Assembly and Characterization of Polyelectrolyte Complex Micelles
Published on: March 2, 2020
Characterization of electrostatic interactions and complex formation of ɣ-poly-glutamic acid (PGA) and
Jorge L Muriel Mundo1, Jinning Liu1, Yunbing Tan1
1Department of Food Science, University of Massachusetts, Amherst, MA 01003, USA.
Abstract:
Complex coacervation is a useful approach for creating biopolymer-based colloidal particles for the oral delivery of bioactives, such as nutraceuticals, vitamins, and pharmaceuticals. In this study, we examined the possibility of using anionic ɣ-poly-glutamic acid (PGA) and cationic ɛ-poly-l-lysine (PLL) to form polyelectrolyte complexes. Initially, the formation and properties of the complexes were characterized using visual observations, UV-visible spectrophotometry, microelectrophoresis (ζ-potential), and isothermal titration calorimetry (ITC). The impact of pH, ionic strength, temperature, and polymer ratio on complex formation was examined. The electrostatic complexes formed had a 1:4 mass ratio of polyanion-to-polycation at saturation (pH 7.4). The surface potential and aggregation stability of the complexes was highly dependent on solution pH (2-12), which was attributed to alterations in the electrical characteristics of the two polyelectrolytes. In particular, insoluble complexes were formed under pH conditions where there was a strong electrostatic attraction between the two polyelectrolytes, whereas soluble complexes were formed when there was only a weak attraction. The addition of salt (≥20 mM NaCl) promoted aggregation of the complexes, presumably due to screening of the electrostatic interactions between them. Conversely, temperature (25-90 °C) did not have a major impact on the stability of the complexes. These results may be useful for the design of effective oral delivery systems for bioactive agents in foods and other products.
Related Concept Videos
Amino acids
EDTA: Chemistry and Properties
Formation of Complex Ions
Ligand Binding Sites
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
Complexation Equilibria: The Chelate Effect
Complexation Equilibria: Overview
The equilibrium constant of the complexation reaction is represented as the formation constant...

