Dehydration-induced structural transitions of proteins in solid state formulations
We propose to study the structural transition of proteins at low water contents and the effect of carbohydrates that are used as pharmaceutical excipients. Our previous Small and Wide angle X-ray scattering experiments on solid state protein samples showed a range of structural information which appears in a form of broad peaks in the q-range 1 - 20 nm-1. The peak at q = 2.5 nm-1 arises from the protein - protein correlations in the crowded amorphous state. The other peak at q = 4.5 nm-1 is however unclear: either it is related to the local packing arrangement, or to a conformational change outlining a domain-domain correlation. In this SANS proposal, using contrast-variation, we aim at disentangle conformational signatures from the packing structure and the localisation of (deuterated) sucrose in solid formulations as well as possible preferential absorption of water around sugar or proteins. This knowledge is crucial to develop understanding the mechanisms of destabilisation of proteins in solid-state formulations.
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The recommended format for citing this dataset in a research publication is in the following format:
PHAN Tuan; CRISTIGLIO Viviana; KOCHERBITOV Vitaly; ROOSEN RUNGE Felix and TERRY Ann. (2020). Dehydration-induced structural transitions of proteins in solid state formulations. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.9-13-941
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This data is not yet public
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