Effect of glassy matrices on the dynamics of embedded proteins: study of the bioprotectant properties of modified monosaccharides.
Bioprotectant glassy matrices have been proven not only to induce a noticeable retardation of protein molecular movements but also to reduce their extent, thus preventing thermal protein degradations. Recently some of us studied the slow dynamic properties of supercooled and glassy levoglucosan (LG) and compared with those of D-glucose (G), a common bioprotectant. The more rigid structure of LG molecule has great impact on the molecular mobility: alpha-relaxation becomes very sensitive to temperature and the secondary relaxation, responsible for the mobility in the glassy state, is suppressed. Quite stikingly, despite its lower Tg (glass transition temperature), LG has been reported to preserve and stabilize freeze-dried proteins better than usual excipients. To investigate how this is related to fast (ps) dynamics, we propose an incoherent neutron scattering investigation vs. T of Lysozyme in G and Lys and LG in dry conditions and at 0.4h hydration degree (D2O). Both G and LG will be deuterated to single out the protein signal from that of the sugar-protein matrix.
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Simone Capaccioli; KAMINSKI kamil; OLLIVIER Jacques; ORECCHINI Andrea; Alessandro Paciaroni; PALUCH Marian; PREVOSTO Daniele and TOMBARI ELPIDIO. (2012). Effect of glassy matrices on the dynamics of embedded proteins: study of the bioprotectant properties of modified monosaccharides.. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.6-05-911
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