Titre :

Influence of urea and guanidine hydrochloride on lysozyme stability and thermal denaturation; a correlation between activity, protein dynamics and conformational changes

Auteur(s) :

Hedoux, Alain [Auteur]
Unité Matériaux et Transformations - UMR 8207 [UMET]
Unité Matériaux et Transformations (UMET) - UMR 8207
Krenzlin, Stefanie [Auteur]
Médicaments et biomatériaux à libération contrôlée: mécanismes et optimisation - Advanced Drug Delivery Systems - U 1008 [MBLC - ADDS]
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]
Leterme-Flament, Marie-Pierre [Auteur]
Advanced Drug Delivery Systems (ADDS) - U1008
Siepmann, Juergen [Auteur]
Médicaments et biomatériaux à libération contrôlée: mécanismes et optimisation - Advanced Drug Delivery Systems - U 1008 [MBLC - ADDS]

Titre de la revue :

Physical Chemistry Chemical Physics

Numéro :

40

Pagination :

13189

Date de publication :

2010

ISSN :

1463-9076

Discipline(s) HAL :

Physique [physics]/Matière Condensée [cond-mat]/Systèmes désordonnés et réseaux de neurones [cond-mat.dis-nn]
Physique [physics]/Matière Condensée [cond-mat]/Science des matériaux [cond-mat.mtrl-sci]
Physique [physics]/Matière Condensée [cond-mat]/Matière Molle [cond-mat.soft]
Sciences du Vivant [q-bio]

Résumé en anglais : [en]

The effect of urea and guanidine hydrochloride (GuHCl) on lysozyme stability has been investigated using activity measurements, microcalorimetry and Raman spectroscopy in the low-frequency and amide I regions. Raman ...
Lire la suite >The effect of urea and guanidine hydrochloride (GuHCl) on lysozyme stability has been investigated using activity measurements, microcalorimetry and Raman spectroscopy in the low-frequency and amide I regions. Raman investigations on lysozyme dissolved in H2O and D2O in the presence of up to 10 M denaturants have revealed direct binding between the protein and both denaturants. The analysis of isotopic exchanges in the amide I region allows the identification of binding sites as hydrophilic and hydrophobic groups, respectively, for urea and GuHCl. The weak loss of activity of lysozyme in the presence of urea (∼15% maximum) is mainly assigned to a transformation of the tertiary structure corresponding to a molten globule state without unfolding of α-helix structures, in contrast to GuHCl which clearly induces conformational changes, associated with a larger loss of activity (40% maximum). The denaturing power of urea and guanidine hydrochloride on lysozyme has been related to the solvent and protein dynamics, reflecting direct interaction between denaturants and protein. It clearly appears that solvent dynamics control protein dynamics, and the significant hardening of the dynamics of GuHCl aqueous solutions is considered responsible for its important denaturing power. The comparison between the low-frequency spectra of solvents and lysozyme aqueous solutions in the absence and presence of different types of additives (urea, GuHCl, trehalose) reveals the Raman signature of the hydration water dynamics. This comparison points out the exclusion of trehalose around the protein surface.Lire moins >

Langue :

Anglais

Audience :

Internationale

Vulgarisation :

Non

Établissement(s) :

Université de Lille
ENSCL
CHU Lille
CNRS
INRA
Inserm

Collections :

• Advanced Drug Delivery Systems (ADDS) - U1008
• Unité Matériaux et Transformations (UMET) - UMR 8207

Équipe(s) de recherche :

Matériaux Moléculaires et Thérapeutiques

Date de dépôt :

2019-05-16T15:14:53Z
2021-06-23T13:33:19Z
2021-09-29T10:42:21Z