Influence of sorbitol on protein crowding in solution and freeze-concentrated phases

Influence of sorbitol on protein crowding in solution and freeze-concentrated phases

Small-angle neutron scattering was employed to study protein crowding under freezing conditions that mimic those used in pharmaceutical processing. The results demonstrate that, although there is an increase in heterogeneity as the temperature is reduced, sorbitol reduces protein crowding in both so...

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Bibliographic Details
Published in:Soft matter Vol. 10; no. 23; p. 4056
Main Authors: Khodadadi, S, Clark, N J, McAuley, A, Cristiglio, V, Curtis, J E, Shalaev, E Y, Krueger, S
Format: Journal Article
Language:English
Published: England 21-06-2014
Subjects:
Muramidase - chemistry
Muramidase - metabolism
Neutron Diffraction
Proteins - chemistry
Proteins - metabolism
Scattering, Small Angle
Solutions - chemistry
Sorbitol - chemistry
Temperature
Water - chemistry
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Summary:Small-angle neutron scattering was employed to study protein crowding under freezing conditions that mimic those used in pharmaceutical processing. The results demonstrate that, although there is an increase in heterogeneity as the temperature is reduced, sorbitol reduces protein crowding in both solution and freeze-concentrated phases, thus protecting the protein from forming oligomers or irreversible aggregates.
ISSN:1744-6848
DOI:10.1039/c4sm00600c