Khodadadi, S.
, Clark, N.
, McAuley, A.
, Cristiglio, V.
, Curtis, J.
, Shalaev, E.
and Krueger, S.
(2014),
Influence Of Sorbitol on Protein Crowding in Solution and Freeze-Concentrated Phases, Soft Matter, [online], https://tsapps.nist.gov/publication/get_pdf.cfm?pub_id=915075
(Accessed April 19, 2024)
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Influence Of Sorbitol on Protein Crowding in Solution and Freeze-Concentrated Phases
Published
Author(s)
Sheila Khodadadi, , Arnold McAuley, Viviana Cristiglio, , Evgenyi Y. Shalaev,
Abstract
Protein stability during processing and storage is of great challenge for biotechnology and pharmaceutical industries. Polyhydroxy compounds are well-known cryo- and lyo-protectors, which minimize destabilization of proteins and biological systems during freeze-drying process. However, freeze-destabilization of proteins is commonly observed even in the presence of these components. In this letter, small-angle neutron scattering was employed to investigate protein crowding in freeze-concentrated solutions of model systems representing pharmaceutical processing conditions in the temperature range of 298 °K to 100 °K. The results demonstrate an increase in large-scale heterogeneity upon cooling to the glass transition and below, as well as two populations of clustered proteins in the freeze-concentrated solution. The interaction distance between proteins is larger in the presence of sorbitol as cryo- lyo-protector than that found in sorbitol-free systems.Citation
Soft Matter
Volume
10
Pub Type
Journals
Download Paper
Keywords
protein interaction, aggregation, amorphous, freeze-drying, small-angle neutron scattering (SANS), differential scanning calorimetry (DSC)
Citation
Created March 30, 2014, Updated October 12, 2021