Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Warner, Nina, Osojnik Črnivec, Ilja Gasan, Rana, Vijay Kumar, Cruz, Menandro, Scherman, Oren A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9000278/
https://www.ncbi.nlm.nih.gov/pubmed/35408595
http://dx.doi.org/10.3390/molecules27072197
_version_ 1784685394959269888
author Warner, Nina
Osojnik Črnivec, Ilja Gasan
Rana, Vijay Kumar
Cruz, Menandro
Scherman, Oren A.
author_facet Warner, Nina
Osojnik Črnivec, Ilja Gasan
Rana, Vijay Kumar
Cruz, Menandro
Scherman, Oren A.
author_sort Warner, Nina
collection PubMed
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 [Formula: see text]) under relevant feed buffer conditions (pH and ionic strength) and that the predictive power of D [Formula: see text] is improved when measured at the spray dryer outlet temperature compared to room temperature ([Formula: see text] = 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.
format Online
Article
Text
id pubmed-9000278
institution National Center for Biotechnology Information
language English
publishDate 2022
publisher MDPI
record_format MEDLINE/PubMed
spelling pubmed-90002782022-04-12 A Platform Approach to Protein Encapsulates with Controllable Surface Chemistry Warner, Nina Osojnik Črnivec, Ilja Gasan Rana, Vijay Kumar Cruz, Menandro Scherman, Oren A. Molecules Article 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 [Formula: see text]) under relevant feed buffer conditions (pH and ionic strength) and that the predictive power of D [Formula: see text] is improved when measured at the spray dryer outlet temperature compared to room temperature ([Formula: see text] = 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. MDPI 2022-03-28 /pmc/articles/PMC9000278/ /pubmed/35408595 http://dx.doi.org/10.3390/molecules27072197 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Warner, Nina
Osojnik Črnivec, Ilja Gasan
Rana, Vijay Kumar
Cruz, Menandro
Scherman, Oren A.
A Platform Approach to Protein Encapsulates with Controllable Surface Chemistry
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 Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9000278/
https://www.ncbi.nlm.nih.gov/pubmed/35408595
http://dx.doi.org/10.3390/molecules27072197
work_keys_str_mv AT warnernina aplatformapproachtoproteinencapsulateswithcontrollablesurfacechemistry
AT osojnikcrniveciljagasan aplatformapproachtoproteinencapsulateswithcontrollablesurfacechemistry
AT ranavijaykumar aplatformapproachtoproteinencapsulateswithcontrollablesurfacechemistry
AT cruzmenandro aplatformapproachtoproteinencapsulateswithcontrollablesurfacechemistry
AT schermanorena aplatformapproachtoproteinencapsulateswithcontrollablesurfacechemistry
AT warnernina platformapproachtoproteinencapsulateswithcontrollablesurfacechemistry
AT osojnikcrniveciljagasan platformapproachtoproteinencapsulateswithcontrollablesurfacechemistry
AT ranavijaykumar platformapproachtoproteinencapsulateswithcontrollablesurfacechemistry
AT cruzmenandro platformapproachtoproteinencapsulateswithcontrollablesurfacechemistry
AT schermanorena platformapproachtoproteinencapsulateswithcontrollablesurfacechemistry