Nanoencapsulation as a General Solution for Lyophilization of Labile Substrates

Protein macromolecules occur naturally at the nanoscale. The use of a dedicated nanoparticle as a lyophilization excipient, however, has not been reported. Because biopolymeric and lipid nanoparticles often denature protein macromolecules and commonly lack the structural rigidity to survive the free...
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Autor*in:	Girish Vallerinteavide Mavelli [verfasserIn] Samira Sadeghi [verfasserIn] Siddhesh Sujit Vaidya [verfasserIn] Shik Nie Kong [verfasserIn] Chester Lee Drum [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2021

Schlagwörter:	lyophilization freeze-drying thermostable exoshells tES HRP

Übergeordnetes Werk:	In: Pharmaceutics - MDPI AG, 2010, 13(2021), 11, p 1790
Übergeordnetes Werk:	volume:13 ; year:2021 ; number:11, p 1790

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.3390/pharmaceutics13111790

Katalog-ID:	DOAJ013333232

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520			\|a Protein macromolecules occur naturally at the nanoscale. The use of a dedicated nanoparticle as a lyophilization excipient, however, has not been reported. Because biopolymeric and lipid nanoparticles often denature protein macromolecules and commonly lack the structural rigidity to survive the freeze-drying process, we hypothesized that surrounding an individual protein substrate with a nanoscale, thermostable exoshell (tES) would prevent aggregation and protect the substrate from denaturation during freezing, sublimation, and storage. We systematically investigated the properties of tES, including secondary structure and its homogeneity, throughout the process of lyophilization and found that tES have a near 100% recovery following aqueous reconstitution. We then tested the hypothesis that tES could encapsulate a model substrate, horseradish peroxidase (HRP), using charge complementation and pH-mediated controlled assembly. HRP were encapsulated within the 8 nm internal tES aqueous cavity using a simplified loading procedure. Time-course experiments demonstrated that unprotected HRP loses 95% of activity after 1 month of lyophilized storage. After encapsulation within tES nanoparticles, 70% of HRP activity was recovered, representing a 14-fold improvement and this effect was reproducible across a range of storage temperatures. To our knowledge, these results represent the first reported use of nanoparticle encapsulation to stabilize a functional macromolecule during lyophilization. Thermostable nanoencapsulation may be a useful method for the long-term storage of labile proteins.
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allfieldsSound	10.3390/pharmaceutics13111790 doi (DE-627)DOAJ013333232 (DE-599)DOAJdd763b45a61d413ba6f315325ad32bc4 DE-627 ger DE-627 rakwb eng RS1-441 Girish Vallerinteavide Mavelli verfasserin aut Nanoencapsulation as a General Solution for Lyophilization of Labile Substrates 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Protein macromolecules occur naturally at the nanoscale. The use of a dedicated nanoparticle as a lyophilization excipient, however, has not been reported. Because biopolymeric and lipid nanoparticles often denature protein macromolecules and commonly lack the structural rigidity to survive the freeze-drying process, we hypothesized that surrounding an individual protein substrate with a nanoscale, thermostable exoshell (tES) would prevent aggregation and protect the substrate from denaturation during freezing, sublimation, and storage. We systematically investigated the properties of tES, including secondary structure and its homogeneity, throughout the process of lyophilization and found that tES have a near 100% recovery following aqueous reconstitution. We then tested the hypothesis that tES could encapsulate a model substrate, horseradish peroxidase (HRP), using charge complementation and pH-mediated controlled assembly. HRP were encapsulated within the 8 nm internal tES aqueous cavity using a simplified loading procedure. Time-course experiments demonstrated that unprotected HRP loses 95% of activity after 1 month of lyophilized storage. After encapsulation within tES nanoparticles, 70% of HRP activity was recovered, representing a 14-fold improvement and this effect was reproducible across a range of storage temperatures. To our knowledge, these results represent the first reported use of nanoparticle encapsulation to stabilize a functional macromolecule during lyophilization. Thermostable nanoencapsulation may be a useful method for the long-term storage of labile proteins. lyophilization freeze-drying thermostable exoshells tES HRP Pharmacy and materia medica Samira Sadeghi verfasserin aut Siddhesh Sujit Vaidya verfasserin aut Shik Nie Kong verfasserin aut Chester Lee Drum verfasserin aut In Pharmaceutics MDPI AG, 2010 13(2021), 11, p 1790 (DE-627)614096529 (DE-600)2527217-2 19994923 nnns volume:13 year:2021 number:11, p 1790 https://doi.org/10.3390/pharmaceutics13111790 kostenfrei https://doaj.org/article/dd763b45a61d413ba6f315325ad32bc4 kostenfrei https://www.mdpi.com/1999-4923/13/11/1790 kostenfrei https://doaj.org/toc/1999-4923 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 13 2021 11, p 1790
language	English
source	In Pharmaceutics 13(2021), 11, p 1790 volume:13 year:2021 number:11, p 1790
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container_title	Pharmaceutics
authorswithroles_txt_mv	Girish Vallerinteavide Mavelli @@aut@@ Samira Sadeghi @@aut@@ Siddhesh Sujit Vaidya @@aut@@ Shik Nie Kong @@aut@@ Chester Lee Drum @@aut@@
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callnumber-first	R - Medicine
author	Girish Vallerinteavide Mavelli
spellingShingle	Girish Vallerinteavide Mavelli misc RS1-441 misc lyophilization misc freeze-drying misc thermostable exoshells misc tES misc HRP misc Pharmacy and materia medica Nanoencapsulation as a General Solution for Lyophilization of Labile Substrates
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topic_title	RS1-441 Nanoencapsulation as a General Solution for Lyophilization of Labile Substrates lyophilization freeze-drying thermostable exoshells tES HRP
topic	misc RS1-441 misc lyophilization misc freeze-drying misc thermostable exoshells misc tES misc HRP misc Pharmacy and materia medica
topic_unstemmed	misc RS1-441 misc lyophilization misc freeze-drying misc thermostable exoshells misc tES misc HRP misc Pharmacy and materia medica
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title	Nanoencapsulation as a General Solution for Lyophilization of Labile Substrates
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title_full	Nanoencapsulation as a General Solution for Lyophilization of Labile Substrates
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title_sort	nanoencapsulation as a general solution for lyophilization of labile substrates
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title_auth	Nanoencapsulation as a General Solution for Lyophilization of Labile Substrates
abstract	Protein macromolecules occur naturally at the nanoscale. The use of a dedicated nanoparticle as a lyophilization excipient, however, has not been reported. Because biopolymeric and lipid nanoparticles often denature protein macromolecules and commonly lack the structural rigidity to survive the freeze-drying process, we hypothesized that surrounding an individual protein substrate with a nanoscale, thermostable exoshell (tES) would prevent aggregation and protect the substrate from denaturation during freezing, sublimation, and storage. We systematically investigated the properties of tES, including secondary structure and its homogeneity, throughout the process of lyophilization and found that tES have a near 100% recovery following aqueous reconstitution. We then tested the hypothesis that tES could encapsulate a model substrate, horseradish peroxidase (HRP), using charge complementation and pH-mediated controlled assembly. HRP were encapsulated within the 8 nm internal tES aqueous cavity using a simplified loading procedure. Time-course experiments demonstrated that unprotected HRP loses 95% of activity after 1 month of lyophilized storage. After encapsulation within tES nanoparticles, 70% of HRP activity was recovered, representing a 14-fold improvement and this effect was reproducible across a range of storage temperatures. To our knowledge, these results represent the first reported use of nanoparticle encapsulation to stabilize a functional macromolecule during lyophilization. Thermostable nanoencapsulation may be a useful method for the long-term storage of labile proteins.
abstractGer	Protein macromolecules occur naturally at the nanoscale. The use of a dedicated nanoparticle as a lyophilization excipient, however, has not been reported. Because biopolymeric and lipid nanoparticles often denature protein macromolecules and commonly lack the structural rigidity to survive the freeze-drying process, we hypothesized that surrounding an individual protein substrate with a nanoscale, thermostable exoshell (tES) would prevent aggregation and protect the substrate from denaturation during freezing, sublimation, and storage. We systematically investigated the properties of tES, including secondary structure and its homogeneity, throughout the process of lyophilization and found that tES have a near 100% recovery following aqueous reconstitution. We then tested the hypothesis that tES could encapsulate a model substrate, horseradish peroxidase (HRP), using charge complementation and pH-mediated controlled assembly. HRP were encapsulated within the 8 nm internal tES aqueous cavity using a simplified loading procedure. Time-course experiments demonstrated that unprotected HRP loses 95% of activity after 1 month of lyophilized storage. After encapsulation within tES nanoparticles, 70% of HRP activity was recovered, representing a 14-fold improvement and this effect was reproducible across a range of storage temperatures. To our knowledge, these results represent the first reported use of nanoparticle encapsulation to stabilize a functional macromolecule during lyophilization. Thermostable nanoencapsulation may be a useful method for the long-term storage of labile proteins.
abstract_unstemmed	Protein macromolecules occur naturally at the nanoscale. The use of a dedicated nanoparticle as a lyophilization excipient, however, has not been reported. Because biopolymeric and lipid nanoparticles often denature protein macromolecules and commonly lack the structural rigidity to survive the freeze-drying process, we hypothesized that surrounding an individual protein substrate with a nanoscale, thermostable exoshell (tES) would prevent aggregation and protect the substrate from denaturation during freezing, sublimation, and storage. We systematically investigated the properties of tES, including secondary structure and its homogeneity, throughout the process of lyophilization and found that tES have a near 100% recovery following aqueous reconstitution. We then tested the hypothesis that tES could encapsulate a model substrate, horseradish peroxidase (HRP), using charge complementation and pH-mediated controlled assembly. HRP were encapsulated within the 8 nm internal tES aqueous cavity using a simplified loading procedure. Time-course experiments demonstrated that unprotected HRP loses 95% of activity after 1 month of lyophilized storage. After encapsulation within tES nanoparticles, 70% of HRP activity was recovered, representing a 14-fold improvement and this effect was reproducible across a range of storage temperatures. To our knowledge, these results represent the first reported use of nanoparticle encapsulation to stabilize a functional macromolecule during lyophilization. Thermostable nanoencapsulation may be a useful method for the long-term storage of labile proteins.
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title_short	Nanoencapsulation as a General Solution for Lyophilization of Labile Substrates
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Nanoencapsulation as a General Solution for Lyophilization of Labile Substrates

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