Influence of the cosolute environment on IgG solution structure analyzed by small-angle X-ray scattering.

ABSTRACT: Small-angle X-ray scattering experiments of two monoclonal antibodies (mAbs) were performed as a function of Hofmeister salt type and concentration including 100 mM Na(2)SO(4), 100-600 mM of NaSCN, or 100-600 mM arginine chloride at pH 6.0 to yield information on the effects of cosolutes on mAb solution conformation and flexibility. Minimal selected ensemble (MSE) procedures used to reconstruct the SAXS form factors revealed that both IgG1 mAbs exist in a conformational equilibrium with two subpopulations that vary in overall shape and size. The "closed" mAb conformation is characterized by a maximum dimension of ∼155 Å and shorter distances between Fab-Fab and Fab-FC domains. The "open" mAb conformation has a maximum dimension of ∼175 Å and an increase in the interdomain distances with co

SUBMITTER: Lilyestrom WG 

PROVIDER: S-EPMC3774592 | biostudies-literature | 2012 Aug

REPOSITORIES: biostudies-literature