Explaining the non-newtonian character of aggregating monoclonal antibody solutions using small-angle neutron scattering.

ABSTRACT: A monoclonal antibody solution displays an increase in low shear rate viscosity upon aggregation after prolonged incubation at 40°C. The morphology and interactions leading to the formation of the aggregates responsible for this non-Newtonian character are resolved using small-angle neutron scattering. Our data show a weak repulsive barrier before proteins aggregate reversibly, unless a favorable contact with high binding energy occurs. Two types of aggregates were identified after incubation at 40°C: oligomers with radius of gyration ∼10 nm and fractal submicrometer particles formed by a slow reaction-limited aggregation process, consistent with monomers colliding many times before finding a favorable strong interaction site. Before incubation, these antibody solutions are Newtonian liqui

SUBMITTER: Castellanos MM 

PROVIDER: S-EPMC4104057 | biostudies-literature | 2014 Jul

REPOSITORIES: biostudies-literature