Trehalose or sucrose; which of the two ...
Type de document :
Article dans une revue scientifique: Article original
URL permanente :
Titre :
Trehalose or sucrose; which of the two should be used for stabilizing proteins in the solid state? A dilemma investigated by in-situ micro-Raman and dielectric relaxation spectroscopies during and after freeze-drying
Auteur(s) :
Starciuc, Tatiana [Auteur]
Unité Matériaux et Transformations - UMR 8207 [UMET]
Unité Matériaux et Transformations (UMET) - UMR 8207
Malfait, Benjamin [Auteur]
Unité Matériaux et Transformations - UMR 8207 [UMET]
Unité Matériaux et Transformations (UMET) - UMR 8207
Danede, Florence [Auteur]
Unité Matériaux et Transformations - UMR 8207 [UMET]
Unité Matériaux et Transformations (UMET) - UMR 8207
Paccou, Laurent [Auteur]
Unité Matériaux et Transformations - UMR 8207 [UMET]
Guinet, Yannick [Auteur]
Unité Matériaux et Transformations - UMR 8207 [UMET]
Unité Matériaux et Transformations (UMET) - UMR 8207
T. Correia, Natália [Auteur]
Unité Matériaux et Transformations - UMR 8207 [UMET]
Unité Matériaux et Transformations (UMET) - UMR 8207
Hedoux, Alain [Auteur]
Unité Matériaux et Transformations - UMR 8207 [UMET]
Unité Matériaux et Transformations (UMET) - UMR 8207
Unité Matériaux et Transformations - UMR 8207 [UMET]
Unité Matériaux et Transformations (UMET) - UMR 8207
Malfait, Benjamin [Auteur]
Unité Matériaux et Transformations - UMR 8207 [UMET]
Unité Matériaux et Transformations (UMET) - UMR 8207
Danede, Florence [Auteur]
Unité Matériaux et Transformations - UMR 8207 [UMET]
Unité Matériaux et Transformations (UMET) - UMR 8207
Paccou, Laurent [Auteur]
Unité Matériaux et Transformations - UMR 8207 [UMET]
Guinet, Yannick [Auteur]
Unité Matériaux et Transformations - UMR 8207 [UMET]
Unité Matériaux et Transformations (UMET) - UMR 8207
T. Correia, Natália [Auteur]
Unité Matériaux et Transformations - UMR 8207 [UMET]
Unité Matériaux et Transformations (UMET) - UMR 8207
Hedoux, Alain [Auteur]
Unité Matériaux et Transformations - UMR 8207 [UMET]
Unité Matériaux et Transformations (UMET) - UMR 8207
Titre de la revue :
Journal of Pharmaceutical Sciences
Numéro :
109
Pagination :
496-504
Date de publication :
2019-01
Mot(s)-clé(s) en anglais :
freeze-drying
bioprotection
lysozyme
disaccharide
protein dynamics
in situ Raman imaging
molecular mobility
bioprotection
lysozyme
disaccharide
protein dynamics
in situ Raman imaging
molecular mobility
Discipline(s) HAL :
Physique [physics]/Matière Condensée [cond-mat]/Science des matériaux [cond-mat.mtrl-sci]
Résumé en anglais : [en]
The bioprotective properties of two disaccharides (sucrose and trehalose) were analyzed during the freeze-drying (FD) process and at the end of the process, in order to better understand the stabilization mechanisms of ...
Lire la suite >The bioprotective properties of two disaccharides (sucrose and trehalose) were analyzed during the freeze-drying (FD) process and at the end of the process, in order to better understand the stabilization mechanisms of proteins in the solid state. In-situ Raman investigations, performed during the FD process have revealed that sucrose was more efficient than trehalose for preserving the secondary structure of lysozyme during FD, especially during the primary drying stage. The lower bioprotective effect of trehalose was interpreted as a consequence of a stronger affinity of this disaccharide to water, which is responsible for a severe phase separation phenomenon during the freezing stage. Dielectric spectroscopy investigations on the dried state of protein formulations have shown the capabilities of trehalose assisted by residual water to reduce the molecular mobility of the vitreous matrix, suggesting that trehalose is more efficient to preserve the protein structure during long-term storage.Lire moins >
Lire la suite >The bioprotective properties of two disaccharides (sucrose and trehalose) were analyzed during the freeze-drying (FD) process and at the end of the process, in order to better understand the stabilization mechanisms of proteins in the solid state. In-situ Raman investigations, performed during the FD process have revealed that sucrose was more efficient than trehalose for preserving the secondary structure of lysozyme during FD, especially during the primary drying stage. The lower bioprotective effect of trehalose was interpreted as a consequence of a stronger affinity of this disaccharide to water, which is responsible for a severe phase separation phenomenon during the freezing stage. Dielectric spectroscopy investigations on the dried state of protein formulations have shown the capabilities of trehalose assisted by residual water to reduce the molecular mobility of the vitreous matrix, suggesting that trehalose is more efficient to preserve the protein structure during long-term storage.Lire moins >
Langue :
Anglais
Comité de lecture :
Oui
Audience :
Internationale
Vulgarisation :
Non
Établissement(s) :
Université de Lille
CNRS
INRA
ENSCL
CNRS
INRA
ENSCL
Collections :
Équipe(s) de recherche :
Matériaux Moléculaires et Thérapeutiques
Date de dépôt :
2020-02-12T13:08:31Z
2020-03-09T10:48:26Z
2022-03-24T13:10:54Z
2020-03-09T10:48:26Z
2022-03-24T13:10:54Z