Protein Encapsulation Using Complex Coacervates: What Nature Has to Teach Us
- 4 May 2020
- Vol. 16 (27), e1907671
- https://doi.org/10.1002/smll.201907671
Abstract
Protein encapsulation is a growing area of interest, particularly in the fields of food science and medicine. The sequestration of protein cargoes is achieved using a variety of methods, each with benefits and drawbacks. One of the most significant challenges associated with protein encapsulation is achieving high loading while maintaining protein viability. This difficulty is exacerbated because many encapsulant systems require the use of organic solvents. By contrast, nature has optimized strategies to compartmentalize and protect proteins inside the cell-a purely aqueous environment. Although the mechanisms whereby aspects of the cytosol is able to stabilize proteins are unknown, the crowded nature of many newly discovered, liquid phase separated "membraneless organelles" that achieve protein compartmentalization suggests that the material environment surrounding the protein may be critical in determining stability. Here, encapsulation strategies based on liquid-liquid phase separation, and complex coacervation in particular, which has many of the key features of the cytoplasm as a material, are reviewed. The literature on protein encapsulation via coacervation is also reviewed and the parameters relevant to creating protein-containing coacervate formulations are discussed. Additionally, potential opportunities associated with the creation of tailored materials to better facilitate protein encapsulation and stabilization are highlighted.Keywords
Funding Information
- PPG Industries
- University of Massachusetts Amherst
- National Science Foundation
This publication has 195 references indexed in Scilit:
- Conformations of intrinsically disordered proteins are influenced by linear sequence distributions of oppositely charged residuesProceedings of the National Academy of Sciences, 2013
- Challenges in nucleic acid-lipid films for transfectionAIChE Journal, 2013
- Aqueous Phase Separation as a Possible Route to Compartmentalization of Biological MoleculesAccounts of Chemical Research, 2012
- The Utility of Hydrogen/Deuterium Exchange Mass Spectrometry in Biopharmaceutical Comparability StudiesJournal of Pharmaceutical Sciences, 2011
- Protein Crowding Tunes Protein StabilityJournal of the American Chemical Society, 2011
- Active liquid-like behavior of nucleoli determines their size and shape in Xenopus laevis oocytesProceedings of the National Academy of Sciences, 2011
- Delivery of Therapeutic ProteinsJournal of Pharmaceutical Sciences, 2010
- Cell penetrating elastin-like polypeptides for therapeutic peptide deliveryAdvanced Drug Delivery Reviews, 2010
- Diffusion, Crowding & Protein Stability in a Dynamic Molecular Model of the Bacterial CytoplasmPLoS Computational Biology, 2010
- Quantitative genome-scale analysis of protein localization in an asymmetric bacteriumProceedings of the National Academy of Sciences, 2009