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Surface Passivation for Single-molecule Protein Studies
Published on: April 24, 2014
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A Platform Approach to Protein Encapsulates with Controllable Surface Chemistry
Nina Warner1, Ilja Gasan Osojnik Črnivec2, Vijay Kumar Rana1
1Melville Laboratory for Polymer Synthesis, Yusuf Hamied Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
Molecules (Basel, Switzerland)
|April 12, 2022
Summary
This study introduces a cost-effective method for protein encapsulation using aqueous spray drying. The findings enable a framework for designing core-shell protein particles without organic solvents, improving stability and release.
Area of Science:
- Biomaterials Engineering
- Particle Engineering
- Drug Delivery Systems
Background:
- Protein encapsulation in core-shell structures is crucial for stability, delivery, and release.
- Current methods are often expensive, poorly scalable, or use harmful organic solvents.
Purpose of the Study:
- To investigate core-shell protein encapsulation using single-feed, aqueous spray drying.
- To develop a predictive model for excipient surface preference in spray-dried particles.
- To establish a design framework for scalable core-shell protein encapsulation.
Main Methods:
- Utilized single-feed, aqueous spray drying, an industrially scalable technique.
- Investigated excipient surface preference based on hydrodynamic diameter (Dh).
- Measured Dh under relevant buffer conditions and at spray dryer outlet temperature.
Main Results:
- Excipient surface preference is predictable by hydrodynamic diameter (Dh) under specific conditions.
- Dh measured at outlet temperature improved predictive power (R2 = 0.64) compared to room temperature (R2 = 0.59).
- Developed an adaptable design framework for core-shell protein encapsulates.
Conclusions:
- Single-feed aqueous spray drying offers a cost-effective, scalable, and solvent-free route for protein encapsulation.
- Hydrodynamic diameter is a key predictor for controlling particle surface composition.
- The proposed framework facilitates the rational design of core-shell protein microstructures.
