Freeze-drying of HI-6-loaded recombinant human serum albumin nanoparticles for improved storage stability
•HI-6 can be stabilised by binding to nanoparticles and lyophilisation.•Trehalose- and sucrose-containing formulations were superior to mannitol.•Nanoparticles enabled HI-6 transport over a porcine endothelial cell model. Severe intoxications with organophosphates require the immediate administratio...
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| Published in | European journal of pharmaceutics and biopharmaceutics Vol. 88; no. 2; pp. 510 - 517 |
|---|---|
| Main Authors | , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Netherlands
Elsevier B.V
01.10.2014
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| Subjects | |
| Online Access | Get full text |
| ISSN | 0939-6411 1873-3441 1873-3441 |
| DOI | 10.1016/j.ejpb.2014.06.008 |
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| Abstract | •HI-6 can be stabilised by binding to nanoparticles and lyophilisation.•Trehalose- and sucrose-containing formulations were superior to mannitol.•Nanoparticles enabled HI-6 transport over a porcine endothelial cell model.
Severe intoxications with organophosphates require the immediate administration of atropine in combination with acetyl cholinesterase (AChE) reactivators such as HI-6. Although this therapy regimen enables the treatment of peripheral symptoms, the blood–brain barrier (BBB) restricts the access of the hydrophilic antidotes to the central nervous system which could lead to a fatal respiratory arrest. Therefore, HI-6-loaded albumin nanoparticles were previously developed to enhance the transport across this barrier and were able to reactivate organophosphate-(OP)-inhibited AChE in an in vitro BBB model. Since HI-6 is known to be moisture-sensitive, the feasibility of freeze-drying of the HI-6-loaded nanoparticles was investigated in the present study using different cryo- and lyoprotectants at different concentrations. Trehalose and sucrose (3%, w/v)-containing formulations were superior to mannitol concerning the physicochemical parameters of the nanoparticles whereas trehalose-containing samples were subject of a prolonged storage stability study at temperatures between −20°C and +40°C for predetermined time intervals. Shelf-life computations of the freeze-dried HI-6 nanoparticle formulations revealed a shelf-life time of 18months when stored at −20°C. The formulations’ efficacy was proven in vitro by reactivation of OP-inhibited AChE after transport over a porcine brain capillary endothelial cell layer model. |
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| AbstractList | •HI-6 can be stabilised by binding to nanoparticles and lyophilisation.•Trehalose- and sucrose-containing formulations were superior to mannitol.•Nanoparticles enabled HI-6 transport over a porcine endothelial cell model.
Severe intoxications with organophosphates require the immediate administration of atropine in combination with acetyl cholinesterase (AChE) reactivators such as HI-6. Although this therapy regimen enables the treatment of peripheral symptoms, the blood–brain barrier (BBB) restricts the access of the hydrophilic antidotes to the central nervous system which could lead to a fatal respiratory arrest. Therefore, HI-6-loaded albumin nanoparticles were previously developed to enhance the transport across this barrier and were able to reactivate organophosphate-(OP)-inhibited AChE in an in vitro BBB model. Since HI-6 is known to be moisture-sensitive, the feasibility of freeze-drying of the HI-6-loaded nanoparticles was investigated in the present study using different cryo- and lyoprotectants at different concentrations. Trehalose and sucrose (3%, w/v)-containing formulations were superior to mannitol concerning the physicochemical parameters of the nanoparticles whereas trehalose-containing samples were subject of a prolonged storage stability study at temperatures between −20°C and +40°C for predetermined time intervals. Shelf-life computations of the freeze-dried HI-6 nanoparticle formulations revealed a shelf-life time of 18months when stored at −20°C. The formulations’ efficacy was proven in vitro by reactivation of OP-inhibited AChE after transport over a porcine brain capillary endothelial cell layer model. Severe intoxications with organophosphates require the immediate administration of atropine in combination with acetyl cholinesterase (AChE) reactivators such as HI-6. Although this therapy regimen enables the treatment of peripheral symptoms, the blood-brain barrier (BBB) restricts the access of the hydrophilic antidotes to the central nervous system which could lead to a fatal respiratory arrest. Therefore, HI-6-loaded albumin nanoparticles were previously developed to enhance the transport across this barrier and were able to reactivate organophosphate-(OP)-inhibited AChE in an in vitro BBB model. Since HI-6 is known to be moisture-sensitive, the feasibility of freeze-drying of the HI-6-loaded nanoparticles was investigated in the present study using different cryo- and lyoprotectants at different concentrations. Trehalose and sucrose (3%, w/v)-containing formulations were superior to mannitol concerning the physicochemical parameters of the nanoparticles whereas trehalose-containing samples were subject of a prolonged storage stability study at temperatures between -20 degree C and +40 degree C for predetermined time intervals. Shelf-life computations of the freeze-dried HI-6 nanoparticle formulations revealed a shelf-life time of 18 months when stored at -20 degree C. The formulations' efficacy was proven in vitro by reactivation of OP-inhibited AChE after transport over a porcine brain capillary endothelial cell layer model. Severe intoxications with organophosphates require the immediate administration of atropine in combination with acetyl cholinesterase (AChE) reactivators such as HI-6. Although this therapy regimen enables the treatment of peripheral symptoms, the blood-brain barrier (BBB) restricts the access of the hydrophilic antidotes to the central nervous system which could lead to a fatal respiratory arrest. Therefore, HI-6-loaded albumin nanoparticles were previously developed to enhance the transport across this barrier and were able to reactivate organophosphate-(OP)-inhibited AChE in an in vitro BBB model. Since HI-6 is known to be moisture-sensitive, the feasibility of freeze-drying of the HI-6-loaded nanoparticles was investigated in the present study using different cryo- and lyoprotectants at different concentrations. Trehalose and sucrose (3%, w/v)-containing formulations were superior to mannitol concerning the physicochemical parameters of the nanoparticles whereas trehalose-containing samples were subject of a prolonged storage stability study at temperatures between -20°C and +40°C for predetermined time intervals. Shelf-life computations of the freeze-dried HI-6 nanoparticle formulations revealed a shelf-life time of 18 months when stored at -20°C. The formulations' efficacy was proven in vitro by reactivation of OP-inhibited AChE after transport over a porcine brain capillary endothelial cell layer model.Severe intoxications with organophosphates require the immediate administration of atropine in combination with acetyl cholinesterase (AChE) reactivators such as HI-6. Although this therapy regimen enables the treatment of peripheral symptoms, the blood-brain barrier (BBB) restricts the access of the hydrophilic antidotes to the central nervous system which could lead to a fatal respiratory arrest. Therefore, HI-6-loaded albumin nanoparticles were previously developed to enhance the transport across this barrier and were able to reactivate organophosphate-(OP)-inhibited AChE in an in vitro BBB model. Since HI-6 is known to be moisture-sensitive, the feasibility of freeze-drying of the HI-6-loaded nanoparticles was investigated in the present study using different cryo- and lyoprotectants at different concentrations. Trehalose and sucrose (3%, w/v)-containing formulations were superior to mannitol concerning the physicochemical parameters of the nanoparticles whereas trehalose-containing samples were subject of a prolonged storage stability study at temperatures between -20°C and +40°C for predetermined time intervals. Shelf-life computations of the freeze-dried HI-6 nanoparticle formulations revealed a shelf-life time of 18 months when stored at -20°C. The formulations' efficacy was proven in vitro by reactivation of OP-inhibited AChE after transport over a porcine brain capillary endothelial cell layer model. Severe intoxications with organophosphates require the immediate administration of atropine in combination with acetyl cholinesterase (AChE) reactivators such as HI-6. Although this therapy regimen enables the treatment of peripheral symptoms, the blood-brain barrier (BBB) restricts the access of the hydrophilic antidotes to the central nervous system which could lead to a fatal respiratory arrest. Therefore, HI-6-loaded albumin nanoparticles were previously developed to enhance the transport across this barrier and were able to reactivate organophosphate-(OP)-inhibited AChE in an in vitro BBB model. Since HI-6 is known to be moisture-sensitive, the feasibility of freeze-drying of the HI-6-loaded nanoparticles was investigated in the present study using different cryo- and lyoprotectants at different concentrations. Trehalose and sucrose (3%, w/v)-containing formulations were superior to mannitol concerning the physicochemical parameters of the nanoparticles whereas trehalose-containing samples were subject of a prolonged storage stability study at temperatures between -20°C and +40°C for predetermined time intervals. Shelf-life computations of the freeze-dried HI-6 nanoparticle formulations revealed a shelf-life time of 18 months when stored at -20°C. The formulations' efficacy was proven in vitro by reactivation of OP-inhibited AChE after transport over a porcine brain capillary endothelial cell layer model. |
| Author | von Briesen, Hagen Wien, Sascha Kreuter, Jörg Worek, Franz Wagner, Sylvia Dadparvar, Miriam |
| Author_xml | – sequence: 1 givenname: Miriam surname: Dadparvar fullname: Dadparvar, Miriam organization: Institute of Pharmaceutical Technology, Johann Wolfgang Goethe University, Frankfurt am Main, Germany – sequence: 2 givenname: Sylvia surname: Wagner fullname: Wagner, Sylvia organization: Department of Cell Biology & Applied Virology, Fraunhofer Institute for Biomedical Engineering, St. Ingbert, Germany – sequence: 3 givenname: Sascha surname: Wien fullname: Wien, Sascha organization: Department of Cell Biology & Applied Virology, Fraunhofer Institute for Biomedical Engineering, St. Ingbert, Germany – sequence: 4 givenname: Franz surname: Worek fullname: Worek, Franz organization: Bundeswehr Institute of Pharmacology and Toxicology, Munich, Germany – sequence: 5 givenname: Hagen surname: von Briesen fullname: von Briesen, Hagen organization: Department of Cell Biology & Applied Virology, Fraunhofer Institute for Biomedical Engineering, St. Ingbert, Germany – sequence: 6 givenname: Jörg surname: Kreuter fullname: Kreuter, Jörg email: kreuter@em.uni-frankfurt.de organization: Institute of Pharmaceutical Technology, Johann Wolfgang Goethe University, Frankfurt am Main, Germany |
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| Copyright | 2014 Elsevier B.V. Copyright © 2014 Elsevier B.V. All rights reserved. |
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| Keywords | Nanoparticles Oximes Storage stability Organophosphate intoxication Blood–brain barrier (BBB) Drug delivery HI-6 Freeze-drying Recombinant human serum albumin |
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| Snippet | •HI-6 can be stabilised by binding to nanoparticles and lyophilisation.•Trehalose- and sucrose-containing formulations were superior to mannitol.•Nanoparticles... Severe intoxications with organophosphates require the immediate administration of atropine in combination with acetyl cholinesterase (AChE) reactivators such... |
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| SubjectTerms | Blood-Brain Barrier Blood–brain barrier (BBB) Drug delivery Drug Stability Feasibility Studies Freeze Drying HI-6 Humans In Vitro Techniques Microscopy, Electron, Scanning Nanoparticles Organophosphate intoxication Oximes Recombinant human serum albumin Recombinant Proteins - chemistry Serum Albumin - chemistry Storage stability |
| Title | Freeze-drying of HI-6-loaded recombinant human serum albumin nanoparticles for improved storage stability |
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