title: Influence of sorbitol on protein crowding in solution and freeze-concentrated phases.
abstract: 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.
authors.affiliation: Faculty of Applied Sciences, Delft University of Technology, Delft, The Netherlands. s.khodadadi@tudelft.nl.
authors.forename: S
authors.initials: S
authors.lastname: Khodadadi
authors.forename: N J
authors.initials: NJ
authors.lastname: Clark
authors.forename: A
authors.initials: A
authors.lastname: McAuley
authors.forename: V
authors.initials: V
authors.lastname: Cristiglio
authors.forename: J E
authors.initials: JE
authors.lastname: Curtis
authors.forename: E Y
authors.initials: EY
authors.lastname: Shalaev
authors.forename: S
authors.initials: S
authors.lastname: Krueger
mesh_terms: D009113:Muramidase / Q000737:chemistry / Q000378:metabolism; D033363:Neutron Diffraction; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D053838:Scattering, Small Angle; D012996:Solutions / Q000737:chemistry; D013012:Sorbitol / Q000737:chemistry*; D013696:Temperature; D014867:Water / Q000737:chemistry
chemical_list: D011506:Proteins; D012996:Solutions; D014867:Water; D013012:Sorbitol; D009113:Muramidase