Hydrophobically modified alginate hydrogels as protein carriers with specific controlled release properties.
Identifieur interne : 000191 ( PubMed/Curation ); précédent : 000190; suivant : 000192Hydrophobically modified alginate hydrogels as protein carriers with specific controlled release properties.
Auteurs : M. Leonard [France] ; M Rastello De Boisseson ; P. Hubert ; F. Dalençon ; E. DellacherieSource :
- Journal of controlled release : official journal of the Controlled Release Society [ 0168-3659 ] ; 2004.
Descripteurs français
- KwdFr :
- Alginates (), Animaux, Calendrier vaccinal, Chimie physique, Concentration en ions d'hydrogène, Fluorescéine-5-isothiocyanate, Helicobacter pylori (immunologie), Hydrogels (), Hémoglobines (immunologie), Immunisation, Immunoglobuline G (biosynthèse), Microsphères, Protéines (administration et posologie), Protéines (pharmacocinétique), Préparation de médicament, Préparations à action retardée, Souris, Sérumalbumine bovine (), Taille de particule, Urease (immunologie), Vaccins antibactériens (immunologie), Vecteurs de médicaments ().
- MESH :
- administration et posologie : Protéines.
- biosynthèse : Immunoglobuline G.
- immunologie : Helicobacter pylori, Hémoglobines, Urease, Vaccins antibactériens.
- pharmacocinétique : Protéines.
- Alginates, Animaux, Calendrier vaccinal, Chimie physique, Concentration en ions d'hydrogène, Fluorescéine-5-isothiocyanate, Hydrogels, Immunisation, Microsphères, Préparation de médicament, Préparations à action retardée, Souris, Sérumalbumine bovine, Taille de particule, Vecteurs de médicaments.
English descriptors
- KwdEn :
- Alginates (chemistry), Animals, Bacterial Vaccines (immunology), Chemistry, Physical, Delayed-Action Preparations, Drug Carriers (chemistry), Drug Compounding, Fluorescein-5-isothiocyanate, Helicobacter pylori (immunology), Hemoglobins (immunology), Hydrogels (chemistry), Hydrogen-Ion Concentration, Immunization, Immunization Schedule, Immunoglobulin G (biosynthesis), Mice, Microspheres, Particle Size, Physicochemical Phenomena, Proteins (administration & dosage), Proteins (pharmacokinetics), Serum Albumin, Bovine (chemistry), Urease (immunology).
- MESH :
- chemical , administration & dosage : Proteins.
- chemical , biosynthesis : Immunoglobulin G.
- chemical , chemistry : Alginates, Drug Carriers, Hydrogels, Serum Albumin, Bovine.
- chemical , immunology : Bacterial Vaccines, Hemoglobins, Urease.
- immunology : Helicobacter pylori.
- chemical , pharmacokinetics : Proteins.
- Animals, Chemistry, Physical, Delayed-Action Preparations, Drug Compounding, Fluorescein-5-isothiocyanate, Hydrogen-Ion Concentration, Immunization, Immunization Schedule, Mice, Microspheres, Particle Size, Physicochemical Phenomena.
Abstract
Amphiphilic derivatives of sodium alginate, prepared by chemical covalent binding of long alkyl chains onto the polysaccharide backbone via ester functions, form strong hydrogels in aqueous solutions. The shear-thinning and thixotropic behaviors of these hydrogels have been exploited to prepare particles (millimetric beads or microparticles) by dispersion in sodium chloride solutions. This all-aqueous procedure was used for the encapsulation of model proteins, such as bovine serum albumin (BSA) and human hemoglobin (Hb), or of a vaccine protein (Helicobacter pylori (H. pylori) urease). In all cases, the encapsulation yields were very high (70-100%). No release of model proteins was observed in water within several days, in contrast with protein-loaded calcium alginate particles, which exhibit an important release within only a few hours. The controlled release of proteins can, however, be achieved by inducing the dissociation of the physical hydrophobic network. This dissociation has been obtained either by addition of surfactants, acting as disrupting agents of intermolecular hydrophobic junctions, or of esterases such as lipases, which hydrolyze the ester bond between alkyl chains and the polysaccharide backbone. The level of immunization against H. pylori infection in mice, induced by encapsulated urease administrated by either systemic or mucosal routes, was also assessed.
DOI: 10.1016/j.jconrel.2004.05.009
PubMed: 15312995
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pubmed:15312995Le document en format XML
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<term>Animals</term>
<term>Bacterial Vaccines (immunology)</term>
<term>Chemistry, Physical</term>
<term>Delayed-Action Preparations</term>
<term>Drug Carriers (chemistry)</term>
<term>Drug Compounding</term>
<term>Fluorescein-5-isothiocyanate</term>
<term>Helicobacter pylori (immunology)</term>
<term>Hemoglobins (immunology)</term>
<term>Hydrogels (chemistry)</term>
<term>Hydrogen-Ion Concentration</term>
<term>Immunization</term>
<term>Immunization Schedule</term>
<term>Immunoglobulin G (biosynthesis)</term>
<term>Mice</term>
<term>Microspheres</term>
<term>Particle Size</term>
<term>Physicochemical Phenomena</term>
<term>Proteins (administration & dosage)</term>
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<term>Animaux</term>
<term>Calendrier vaccinal</term>
<term>Chimie physique</term>
<term>Concentration en ions d'hydrogène</term>
<term>Fluorescéine-5-isothiocyanate</term>
<term>Helicobacter pylori (immunologie)</term>
<term>Hydrogels ()</term>
<term>Hémoglobines (immunologie)</term>
<term>Immunisation</term>
<term>Immunoglobuline G (biosynthèse)</term>
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<term>Protéines (administration et posologie)</term>
<term>Protéines (pharmacocinétique)</term>
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<term>Vaccins antibactériens (immunologie)</term>
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<term>Drug Carriers</term>
<term>Hydrogels</term>
<term>Serum Albumin, Bovine</term>
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<term>Urease</term>
<term>Vaccins antibactériens</term>
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<term>Chemistry, Physical</term>
<term>Delayed-Action Preparations</term>
<term>Drug Compounding</term>
<term>Fluorescein-5-isothiocyanate</term>
<term>Hydrogen-Ion Concentration</term>
<term>Immunization</term>
<term>Immunization Schedule</term>
<term>Mice</term>
<term>Microspheres</term>
<term>Particle Size</term>
<term>Physicochemical Phenomena</term>
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<term>Animaux</term>
<term>Calendrier vaccinal</term>
<term>Chimie physique</term>
<term>Concentration en ions d'hydrogène</term>
<term>Fluorescéine-5-isothiocyanate</term>
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<term>Microsphères</term>
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<term>Préparations à action retardée</term>
<term>Souris</term>
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<front><div type="abstract" xml:lang="en">Amphiphilic derivatives of sodium alginate, prepared by chemical covalent binding of long alkyl chains onto the polysaccharide backbone via ester functions, form strong hydrogels in aqueous solutions. The shear-thinning and thixotropic behaviors of these hydrogels have been exploited to prepare particles (millimetric beads or microparticles) by dispersion in sodium chloride solutions. This all-aqueous procedure was used for the encapsulation of model proteins, such as bovine serum albumin (BSA) and human hemoglobin (Hb), or of a vaccine protein (Helicobacter pylori (H. pylori) urease). In all cases, the encapsulation yields were very high (70-100%). No release of model proteins was observed in water within several days, in contrast with protein-loaded calcium alginate particles, which exhibit an important release within only a few hours. The controlled release of proteins can, however, be achieved by inducing the dissociation of the physical hydrophobic network. This dissociation has been obtained either by addition of surfactants, acting as disrupting agents of intermolecular hydrophobic junctions, or of esterases such as lipases, which hydrolyze the ester bond between alkyl chains and the polysaccharide backbone. The level of immunization against H. pylori infection in mice, induced by encapsulated urease administrated by either systemic or mucosal routes, was also assessed.</div>
</front>
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<Abstract><AbstractText>Amphiphilic derivatives of sodium alginate, prepared by chemical covalent binding of long alkyl chains onto the polysaccharide backbone via ester functions, form strong hydrogels in aqueous solutions. The shear-thinning and thixotropic behaviors of these hydrogels have been exploited to prepare particles (millimetric beads or microparticles) by dispersion in sodium chloride solutions. This all-aqueous procedure was used for the encapsulation of model proteins, such as bovine serum albumin (BSA) and human hemoglobin (Hb), or of a vaccine protein (Helicobacter pylori (H. pylori) urease). In all cases, the encapsulation yields were very high (70-100%). No release of model proteins was observed in water within several days, in contrast with protein-loaded calcium alginate particles, which exhibit an important release within only a few hours. The controlled release of proteins can, however, be achieved by inducing the dissociation of the physical hydrophobic network. This dissociation has been obtained either by addition of surfactants, acting as disrupting agents of intermolecular hydrophobic junctions, or of esterases such as lipases, which hydrolyze the ester bond between alkyl chains and the polysaccharide backbone. The level of immunization against H. pylori infection in mice, induced by encapsulated urease administrated by either systemic or mucosal routes, was also assessed.</AbstractText>
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