Optimization of Hemoglobin Encapsulation within PLGA Nanoparticles and Their Investigation as Potential Oxygen Carriers

Hemoglobin (Hb)-based oxygen carriers (HBOCs) display the excellent oxygen-carrying properties of red blood cells, while overcoming some of the limitations of donor blood. Various encapsulation platforms have been explored to prepare HBOCs which aim to avoid or minimize the adverse effects caused by...

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Autores principales:	Clara Coll-Satue, Michelle Maria Theresia Jansman, Peter Waaben Thulstrup, Leticia Hosta-Rigau
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	blood substitutes double emulsification hemoglobin-based oxygen carriers PLGA nanoparticles protein stability trehalose Pharmacy and materia medica RS1-441
Acceso en línea:	https://doaj.org/article/53ad225f5cf6415280b4dbb5c5d02b8d
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spelling	oai:doaj.org-article:53ad225f5cf6415280b4dbb5c5d02b8d2021-11-25T18:42:22ZOptimization of Hemoglobin Encapsulation within PLGA Nanoparticles and Their Investigation as Potential Oxygen Carriers10.3390/pharmaceutics131119581999-4923https://doaj.org/article/53ad225f5cf6415280b4dbb5c5d02b8d2021-11-01T00:00:00Zhttps://www.mdpi.com/1999-4923/13/11/1958https://doaj.org/toc/1999-4923Hemoglobin (Hb)-based oxygen carriers (HBOCs) display the excellent oxygen-carrying properties of red blood cells, while overcoming some of the limitations of donor blood. Various encapsulation platforms have been explored to prepare HBOCs which aim to avoid or minimize the adverse effects caused by the administration of free Hb. Herein, we entrapped Hb within a poly(lactide-co-glycolide) (PLGA) core, prepared by the double emulsion solvent evaporation method. We study the effect of the concentrations of Hb, PLGA, and emulsifier on the size, polydispersity (PDI), loading capacity (LC), and entrapment efficiency (EE) of the resulting Hb-loaded PLGA nanoparticles (HbNPs). Next, the ability of the HbNPs to reversibly bind and release oxygen was thoroughly evaluated. When needed, trehalose, a well-known protein stabilizer that has never been explored for the fabrication of HBOCs, was incorporated to preserve Hb’s functionality. The optimized formulation had a size of 344 nm, a PDI of 0.172, a LC of 26.9%, and an EE of 40.7%. The HbNPs were imaged by microscopy and were further characterized by FTIR and CD spectroscopy to assess their chemical composition and structure. Finally, the ability of the encapsulated Hb to bind and release oxygen over several rounds was demonstrated, showing the preservation of its functionality.Clara Coll-SatueMichelle Maria Theresia JansmanPeter Waaben ThulstrupLeticia Hosta-RigauMDPI AGarticleblood substitutesdouble emulsificationhemoglobin-based oxygen carriersPLGA nanoparticlesprotein stabilitytrehalosePharmacy and materia medicaRS1-441ENPharmaceutics, Vol 13, Iss 1958, p 1958 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	blood substitutes double emulsification hemoglobin-based oxygen carriers PLGA nanoparticles protein stability trehalose Pharmacy and materia medica RS1-441
spellingShingle	blood substitutes double emulsification hemoglobin-based oxygen carriers PLGA nanoparticles protein stability trehalose Pharmacy and materia medica RS1-441 Clara Coll-Satue Michelle Maria Theresia Jansman Peter Waaben Thulstrup Leticia Hosta-Rigau Optimization of Hemoglobin Encapsulation within PLGA Nanoparticles and Their Investigation as Potential Oxygen Carriers
description	Hemoglobin (Hb)-based oxygen carriers (HBOCs) display the excellent oxygen-carrying properties of red blood cells, while overcoming some of the limitations of donor blood. Various encapsulation platforms have been explored to prepare HBOCs which aim to avoid or minimize the adverse effects caused by the administration of free Hb. Herein, we entrapped Hb within a poly(lactide-co-glycolide) (PLGA) core, prepared by the double emulsion solvent evaporation method. We study the effect of the concentrations of Hb, PLGA, and emulsifier on the size, polydispersity (PDI), loading capacity (LC), and entrapment efficiency (EE) of the resulting Hb-loaded PLGA nanoparticles (HbNPs). Next, the ability of the HbNPs to reversibly bind and release oxygen was thoroughly evaluated. When needed, trehalose, a well-known protein stabilizer that has never been explored for the fabrication of HBOCs, was incorporated to preserve Hb’s functionality. The optimized formulation had a size of 344 nm, a PDI of 0.172, a LC of 26.9%, and an EE of 40.7%. The HbNPs were imaged by microscopy and were further characterized by FTIR and CD spectroscopy to assess their chemical composition and structure. Finally, the ability of the encapsulated Hb to bind and release oxygen over several rounds was demonstrated, showing the preservation of its functionality.
format	article
author	Clara Coll-Satue Michelle Maria Theresia Jansman Peter Waaben Thulstrup Leticia Hosta-Rigau
author_facet	Clara Coll-Satue Michelle Maria Theresia Jansman Peter Waaben Thulstrup Leticia Hosta-Rigau
author_sort	Clara Coll-Satue
title	Optimization of Hemoglobin Encapsulation within PLGA Nanoparticles and Their Investigation as Potential Oxygen Carriers
title_short	Optimization of Hemoglobin Encapsulation within PLGA Nanoparticles and Their Investigation as Potential Oxygen Carriers
title_full	Optimization of Hemoglobin Encapsulation within PLGA Nanoparticles and Their Investigation as Potential Oxygen Carriers
title_fullStr	Optimization of Hemoglobin Encapsulation within PLGA Nanoparticles and Their Investigation as Potential Oxygen Carriers
title_full_unstemmed	Optimization of Hemoglobin Encapsulation within PLGA Nanoparticles and Their Investigation as Potential Oxygen Carriers
title_sort	optimization of hemoglobin encapsulation within plga nanoparticles and their investigation as potential oxygen carriers
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/53ad225f5cf6415280b4dbb5c5d02b8d
work_keys_str_mv	AT claracollsatue optimizationofhemoglobinencapsulationwithinplgananoparticlesandtheirinvestigationaspotentialoxygencarriers AT michellemariatheresiajansman optimizationofhemoglobinencapsulationwithinplgananoparticlesandtheirinvestigationaspotentialoxygencarriers AT peterwaabenthulstrup optimizationofhemoglobinencapsulationwithinplgananoparticlesandtheirinvestigationaspotentialoxygencarriers AT leticiahostarigau optimizationofhemoglobinencapsulationwithinplgananoparticlesandtheirinvestigationaspotentialoxygencarriers
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Optimization of Hemoglobin Encapsulation within PLGA Nanoparticles and Their Investigation as Potential Oxygen Carriers

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