Reference : Effects of monopropanediamino-beta-cyclodextrin on the denaturation process of the hy...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
Effects of monopropanediamino-beta-cyclodextrin on the denaturation process of the hybrid protein BlaPChBD.
Vandevenne, Marylène mailto [Université de Liège > > Centre d'ingénierie des protéines >]
GASPARD, Genevieve [Centre Hospitalier Universitaire de Liège - CHU > > Service d'Informations médico économiques (SIME)]
Belgsir, E. M. [> > > >]
Ramnath, M. [> > > >]
Cenatiempo, Y. [> > > >]
Delneuville, Delphine mailto [Université de Liège - ULg > Département des sciences biomédicales et précliniques > Anatomie et cytologie pathologiques]
Dumoulin, Mireille mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines]
Frère, Jean-Marie mailto [Université de Liège - ULg > Département des sciences de la vie > Enzymologie et repliement des protéines]
Matagne, André mailto [Université de Liège - ULg > Département des sciences de la vie > Macromolécules biologiques]
Galleni, Moreno mailto [> > > >]
Filee, P. [> >]
Biochimica et biophysica acta
Yes (verified by ORBi)
[en] Irreversible accumulation of protein aggregates represents an important problem both in vivo and in vitro. The aggregation of proteins is of critical importance in a wide variety of biomedical situations, ranging from diseases (such as Alzheimer's and Parkinson's diseases) to the production (e.g. inclusion bodies), stability, storage and delivery of protein drugs. beta-Cyclodextrin (beta-CD) is a circular heptasaccharide characterized by a hydrophilic exterior and a hydrophobic interior ring structure. In this research, we studied the effects of a chemically modified beta-CD (BCD07056), on the aggregating and refolding properties of BlaPChBD, a hybrid protein obtained by inserting the chitin binding domain of the human macrophage chitotriosidase into the class A beta-lactamase BlaP from Bacillus licheniformis 749/I during its thermal denaturation. The results show that BCD07056 strongly increases the refolding yield of BlaPChBD after thermal denaturation and constitutes an excellent additive to stabilize the protein over time at room temperature. Our data suggest that BCD07056 acts early in the denaturation process by preventing the formation of an intermediate which leads to an aggregated state. Finally, the role of beta-CD derivatives on the stability of proteins is discussed.
Copyright (c) 2011. Published by Elsevier B.V.

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