Role of amorphous/amorphous and crystal/amorphous water interfaces in cold destabilization of proteins
Sugars and other polyhydroxycompounds are well-known cryo- and lyo-protectors which minimize destabilization of proteins and other biological systems during freeze-drying process. However, freeze-destabilization of proteins is commonly observed even in presence of sugars. There are several mechanisms proposed for freeze-destabilization of proteins, including different freeze-concentration effects, cold-denaturation of protein molecules , and destabilization of proteins due to interfaces between ice crystals and remaining unfrozen solution. In particular, formation of ice per se was shown to have destabilizing effect on protein molecules during freezing. However, details of such destabilizing effect of ice water interfaces have not been studied. In this proposed study, we will investigate water distribution in biologically-relevant glasses, in particular carbohydrate-sugar systems, and its impact on stability of proteins. We also will study the role of water interfaces, by creating different types of the interfaces, and monitoring changes in protein molecules interaction using small angle neutron scattering technique.
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KRUEGER Susan; CICERONE Marcus; CRISTIGLIO Viviana; CURTIS Joseph; GRILLO Isabelle; KHODADADI Sheila and SHALAEV EVGENYI. (2012). Role of amorphous/amorphous and crystal/amorphous water interfaces in cold destabilization of proteins. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-05-408
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