Rapid, Single-Step Protein Encapsulation via Flash NanoPrecipitation
Flash NanoPrecipitation (FNP) is a rapid method for encapsulating hydrophobic materials in polymer nanoparticles with high loading capacity. Encapsulating biologics such as proteins remains a challenge due to their low hydrophobicity (logP < 6) and current methods require multiple processing...
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2019-08-01
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Online Access: | https://www.mdpi.com/2073-4360/11/9/1406 |
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doaj-3b0e662cf83b4b9f978af4ff48d0ba022020-11-24T20:42:49ZengMDPI AGPolymers2073-43602019-08-01119140610.3390/polym11091406polym11091406Rapid, Single-Step Protein Encapsulation via Flash NanoPrecipitationShani L. Levit0Rebecca C. Walker1Christina Tang2Chemical and Life Science Engineering Department, Virginia Commonwealth University, Richmond, VA 23284-3028, USAChemical and Life Science Engineering Department, Virginia Commonwealth University, Richmond, VA 23284-3028, USAChemical and Life Science Engineering Department, Virginia Commonwealth University, Richmond, VA 23284-3028, USAFlash NanoPrecipitation (FNP) is a rapid method for encapsulating hydrophobic materials in polymer nanoparticles with high loading capacity. Encapsulating biologics such as proteins remains a challenge due to their low hydrophobicity (logP < 6) and current methods require multiple processing steps. In this work, we report rapid, single-step protein encapsulation via FNP using bovine serum albumin (BSA) as a model protein. Nanoparticle formation involves complexation and precipitation of protein with tannic acid and stabilization with a cationic polyelectrolyte. Nanoparticle self-assembly is driven by hydrogen bonding and electrostatic interactions. Using this approach, high encapsulation efficiency (up to ~80%) of protein can be achieved. The resulting nanoparticles are stable at physiological pH and ionic strength. Overall, FNP is a rapid, efficient platform for encapsulating proteins for various applications.https://www.mdpi.com/2073-4360/11/9/1406Flash NanoPrecipitationnanoparticlespolyethylenimineself-assemblytannic-acidelectrostatic interactionsprotein encapsulation |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Shani L. Levit Rebecca C. Walker Christina Tang |
spellingShingle |
Shani L. Levit Rebecca C. Walker Christina Tang Rapid, Single-Step Protein Encapsulation via Flash NanoPrecipitation Polymers Flash NanoPrecipitation nanoparticles polyethylenimine self-assembly tannic-acid electrostatic interactions protein encapsulation |
author_facet |
Shani L. Levit Rebecca C. Walker Christina Tang |
author_sort |
Shani L. Levit |
title |
Rapid, Single-Step Protein Encapsulation via Flash NanoPrecipitation |
title_short |
Rapid, Single-Step Protein Encapsulation via Flash NanoPrecipitation |
title_full |
Rapid, Single-Step Protein Encapsulation via Flash NanoPrecipitation |
title_fullStr |
Rapid, Single-Step Protein Encapsulation via Flash NanoPrecipitation |
title_full_unstemmed |
Rapid, Single-Step Protein Encapsulation via Flash NanoPrecipitation |
title_sort |
rapid, single-step protein encapsulation via flash nanoprecipitation |
publisher |
MDPI AG |
series |
Polymers |
issn |
2073-4360 |
publishDate |
2019-08-01 |
description |
Flash NanoPrecipitation (FNP) is a rapid method for encapsulating hydrophobic materials in polymer nanoparticles with high loading capacity. Encapsulating biologics such as proteins remains a challenge due to their low hydrophobicity (logP < 6) and current methods require multiple processing steps. In this work, we report rapid, single-step protein encapsulation via FNP using bovine serum albumin (BSA) as a model protein. Nanoparticle formation involves complexation and precipitation of protein with tannic acid and stabilization with a cationic polyelectrolyte. Nanoparticle self-assembly is driven by hydrogen bonding and electrostatic interactions. Using this approach, high encapsulation efficiency (up to ~80%) of protein can be achieved. The resulting nanoparticles are stable at physiological pH and ionic strength. Overall, FNP is a rapid, efficient platform for encapsulating proteins for various applications. |
topic |
Flash NanoPrecipitation nanoparticles polyethylenimine self-assembly tannic-acid electrostatic interactions protein encapsulation |
url |
https://www.mdpi.com/2073-4360/11/9/1406 |
work_keys_str_mv |
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