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Adding a homopolymer enhances complex coacervate core micelle (C3M) salt stability. However, this competitor molecule unexpectedly causes premature protein release from C3Ms at lower salt concentrations.

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Area of Science:

  • Polymer Science
  • Biotechnology
  • Materials Science

Background:

  • Complex coacervate core micelles (C3Ms) encapsulate charged proteins using oppositely charged diblock copolymers.
  • C3Ms are prone to disintegration in high ionic strength environments.
  • Adding a homopolymer with the same charge as the protein can improve C3M stability.

Purpose of the Study:

  • To investigate the effect of homopolymer addition on protein encapsulation efficiency and salt stability in C3Ms.
  • To analyze the competitive interactions between a protein and a homopolymer during C3M formation.

Main Methods:

  • Utilized fluorescence correlation spectroscopy (FCS) and dynamic light scattering (DLS) to study C3M behavior.
  • Investigated the encapsulation of laccase spore coat protein A (CotA) using a cationic-neutral diblock copolymer (PM2VP-b-PEO) and a negatively charged homopolymer (PSS).

Main Results:

  • DLS confirmed improved salt stability of the three-component C3M system (protein, copolymer, homopolymer) compared to a two-component system.
  • FCS revealed that CotA was released from the three-component C3Ms at lower salt concentrations than C3M dissociation.
  • The homopolymer competed with CotA for encapsulation, leading to earlier protein exclusion.

Conclusions:

  • While homopolymer addition enhances overall micelle salt stability, it also acts as a competitor for protein encapsulation.
  • This competition results in premature release of encapsulated proteins at lower ionic strengths than previously observed.
  • Understanding these competitive dynamics is crucial for designing stable and efficient protein-loaded C3Ms.