Self-Reorganizing Multilayer to Release Free Proteins from Self-Assemblies

Area of Science:

• Materials Science
• Biochemistry
• Chemical Engineering

Background:

• Protein-polyelectrolyte (PE) self-assemblies are crucial for biomaterials and drug delivery.
• Releasing intact proteins from these assemblies often requires complex methods or specific PE properties.

Purpose of the Study:

• To develop a novel, simple method for releasing intact, bioactive proteins from self-assemblies.
• To investigate a pH-triggered reorganization mechanism for protein release.

Main Methods:

• Fabrication of interfacial self-assemblies using a strong polyacid, a protein, and a weak polybase.
• Induction of self-assembly reorganization via a pH shift.
• Assessment of protein bioactivity post-release.

Main Results:

• A pH shift one unit below the weak polybase's pKa induced PE association and protein release.
• The released lysozyme retained up to 50% of its initial bioactivity.
• A control film that did not reorganize retained only 21% bioactivity.

Conclusions:

• The pH-triggered associative mechanism offers a versatile approach for releasing active proteins.
• This method is valuable for developing advanced drug delivery systems and biomaterials.
• The strategy relies on PE association, not altered protein-PE coupling, preserving protein integrity.