Trehalose or sucrose; which of the two ...
Document type :
Article dans une revue scientifique: Article original
Permalink :
Title :
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
Author(s) :
Starciuc, Tatiana [Auteur]
Unité Matériaux et Transformations (UMET) - UMR 8207
Unité Matériaux et Transformations - UMR 8207 [UMET]
Malfait, Benjamin [Auteur]
Unité Matériaux et Transformations (UMET) - UMR 8207
Unité Matériaux et Transformations - UMR 8207 [UMET]
Danede, Florence [Auteur]
Unité Matériaux et Transformations (UMET) - UMR 8207
Unité Matériaux et Transformations - UMR 8207 [UMET]
Paccou, Laurent [Auteur]
Unité Matériaux et Transformations - UMR 8207 [UMET]
Guinet, Yannick [Auteur]
Unité Matériaux et Transformations (UMET) - UMR 8207
Unité Matériaux et Transformations - UMR 8207 [UMET]
T. Correia, Natália [Auteur]
Unité Matériaux et Transformations (UMET) - UMR 8207
Unité Matériaux et Transformations - UMR 8207 [UMET]
Hedoux, Alain [Auteur]
Unité Matériaux et Transformations (UMET) - UMR 8207
Unité Matériaux et Transformations - UMR 8207 [UMET]
Unité Matériaux et Transformations (UMET) - UMR 8207
Unité Matériaux et Transformations - UMR 8207 [UMET]
Malfait, Benjamin [Auteur]
Unité Matériaux et Transformations (UMET) - UMR 8207
Unité Matériaux et Transformations - UMR 8207 [UMET]
Danede, Florence [Auteur]
Unité Matériaux et Transformations (UMET) - UMR 8207
Unité Matériaux et Transformations - UMR 8207 [UMET]
Paccou, Laurent [Auteur]

Unité Matériaux et Transformations - UMR 8207 [UMET]
Guinet, Yannick [Auteur]

Unité Matériaux et Transformations (UMET) - UMR 8207
Unité Matériaux et Transformations - UMR 8207 [UMET]
T. Correia, Natália [Auteur]

Unité Matériaux et Transformations (UMET) - UMR 8207
Unité Matériaux et Transformations - UMR 8207 [UMET]
Hedoux, Alain [Auteur]

Unité Matériaux et Transformations (UMET) - UMR 8207
Unité Matériaux et Transformations - UMR 8207 [UMET]
Journal title :
Journal of Pharmaceutical Sciences
Volume number :
109
Pages :
496-504
Publication date :
2019-01
English keyword(s) :
freeze-drying
bioprotection
lysozyme
disaccharide
protein dynamics
in situ Raman imaging
molecular mobility
bioprotection
lysozyme
disaccharide
protein dynamics
in situ Raman imaging
molecular mobility
HAL domain(s) :
Physique [physics]/Matière Condensée [cond-mat]/Science des matériaux [cond-mat.mtrl-sci]
English abstract : [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 ...
Show more >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.Show less >
Show more >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.Show less >
Language :
Anglais
Peer reviewed article :
Oui
Audience :
Internationale
Popular science :
Non
Administrative institution(s) :
Université de Lille
CNRS
INRA
ENSCL
CNRS
INRA
ENSCL
Collections :
Research team(s) :
Matériaux Moléculaires et Thérapeutiques
Submission date :
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