A Platform Approach to Protein Encapsulates with Controllable Surface Chemistry
The encapsulation of proteins into core-shell structures is a widely utilised strategy for controlling protein stability, delivery and release. Despite the recognised utility of these microstructures, however, core-shell fabrication routes are often too costly or poorly scalable to allow for industr...
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MDPI AG
2022-03-01
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Online Access: | https://www.mdpi.com/1420-3049/27/7/2197 |
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author | Nina Warner Ilja Gasan Osojnik Črnivec Vijay Kumar Rana Menandro Cruz Oren A. Scherman |
author_facet | Nina Warner Ilja Gasan Osojnik Črnivec Vijay Kumar Rana Menandro Cruz Oren A. Scherman |
author_sort | Nina Warner |
collection | DOAJ |
description | The encapsulation of proteins into core-shell structures is a widely utilised strategy for controlling protein stability, delivery and release. Despite the recognised utility of these microstructures, however, core-shell fabrication routes are often too costly or poorly scalable to allow for industrial translation. Furthermore, many scalable routes rely upon emulsion-techniques implicating denaturing or environmentally harmful organic solvents. Herein, we investigate core-shell protein encapsulation through single-feed, aqueous spray drying: a cheap, industrially ubiquitous particle-formation technology in the absence of organic solvents. We show that an excipient’s preference for the surface of the spray dried particle is well-predicted by its hydrodynamic diameter (D<inline-formula><math xmlns="http://www.w3.org/1998/Math/MathML" display="inline"><semantics><msub><mrow></mrow><mi>h</mi></msub></semantics></math></inline-formula>) under relevant feed buffer conditions (pH and ionic strength) and that the predictive power of D<inline-formula><math xmlns="http://www.w3.org/1998/Math/MathML" display="inline"><semantics><msub><mrow></mrow><mi>h</mi></msub></semantics></math></inline-formula> is improved when measured at the spray dryer outlet temperature compared to room temperature (<inline-formula><math xmlns="http://www.w3.org/1998/Math/MathML" display="inline"><semantics><msup><mi mathvariant="normal">R</mi><mn>2</mn></msup></semantics></math></inline-formula> = 0.64 vs. 0.59). Lastly, we leverage these findings to propose an adaptable design framework for fabricating core-shell protein encapsulates by single-feed aqueous spray drying. |
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language | English |
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publishDate | 2022-03-01 |
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series | Molecules |
spelling | doaj.art-df9f027ecf8a4c63bf924a840b75bca82023-11-30T23:40:54ZengMDPI AGMolecules1420-30492022-03-01277219710.3390/molecules27072197A Platform Approach to Protein Encapsulates with Controllable Surface ChemistryNina Warner0Ilja Gasan Osojnik Črnivec1Vijay Kumar Rana2Menandro Cruz3Oren A. Scherman4Melville Laboratory for Polymer Synthesis, Yusuf Hamied Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UKBiotechnical Faculty, University of Ljubljana, Jamnikarjeva 101, SI-1000 Ljubljana, SloveniaMelville Laboratory for Polymer Synthesis, Yusuf Hamied Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UKMelville Laboratory for Polymer Synthesis, Yusuf Hamied Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UKMelville Laboratory for Polymer Synthesis, Yusuf Hamied Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UKThe encapsulation of proteins into core-shell structures is a widely utilised strategy for controlling protein stability, delivery and release. Despite the recognised utility of these microstructures, however, core-shell fabrication routes are often too costly or poorly scalable to allow for industrial translation. Furthermore, many scalable routes rely upon emulsion-techniques implicating denaturing or environmentally harmful organic solvents. Herein, we investigate core-shell protein encapsulation through single-feed, aqueous spray drying: a cheap, industrially ubiquitous particle-formation technology in the absence of organic solvents. We show that an excipient’s preference for the surface of the spray dried particle is well-predicted by its hydrodynamic diameter (D<inline-formula><math xmlns="http://www.w3.org/1998/Math/MathML" display="inline"><semantics><msub><mrow></mrow><mi>h</mi></msub></semantics></math></inline-formula>) under relevant feed buffer conditions (pH and ionic strength) and that the predictive power of D<inline-formula><math xmlns="http://www.w3.org/1998/Math/MathML" display="inline"><semantics><msub><mrow></mrow><mi>h</mi></msub></semantics></math></inline-formula> is improved when measured at the spray dryer outlet temperature compared to room temperature (<inline-formula><math xmlns="http://www.w3.org/1998/Math/MathML" display="inline"><semantics><msup><mi mathvariant="normal">R</mi><mn>2</mn></msup></semantics></math></inline-formula> = 0.64 vs. 0.59). Lastly, we leverage these findings to propose an adaptable design framework for fabricating core-shell protein encapsulates by single-feed aqueous spray drying.https://www.mdpi.com/1420-3049/27/7/2197spray dryproteinencapsulationformulationexcipientcore-shell |
spellingShingle | Nina Warner Ilja Gasan Osojnik Črnivec Vijay Kumar Rana Menandro Cruz Oren A. Scherman A Platform Approach to Protein Encapsulates with Controllable Surface Chemistry Molecules spray dry protein encapsulation formulation excipient core-shell |
title | A Platform Approach to Protein Encapsulates with Controllable Surface Chemistry |
title_full | A Platform Approach to Protein Encapsulates with Controllable Surface Chemistry |
title_fullStr | A Platform Approach to Protein Encapsulates with Controllable Surface Chemistry |
title_full_unstemmed | A Platform Approach to Protein Encapsulates with Controllable Surface Chemistry |
title_short | A Platform Approach to Protein Encapsulates with Controllable Surface Chemistry |
title_sort | platform approach to protein encapsulates with controllable surface chemistry |
topic | spray dry protein encapsulation formulation excipient core-shell |
url | https://www.mdpi.com/1420-3049/27/7/2197 |
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