Rebecca K Brummitt

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Aggregation mechanisms as a function of pH were assessed for the IgG1 antibody described in Part 1 (Brummitt RK, Nesta DP, Chang L, Chase SF, Laue TM, Roberts CJ. Non-native aggregation of an IGG1 antibody in acidic conditions: 1. Unfolding, colloidal interactions, and high molecular weight aggregate formation. J Pharm Sci. In press). Aggregation kinetics(More)
Nonnative aggregation is a common degradation route for therapeutic proteins. Control of aggregate levels inherently requires control and/or prediction of aggregation rates at formulation conditions and storage temperatures of practical interest. Additionally, formulation screening often involves generation of accelerated stability data at one or more(More)
Amyloid aggregates have been hypothesized as a global low free energy state for proteins at finite concentrations. Near its midpoint unfolding temperature, α-chymotrypsinogen A (aCgn) spontaneously forms amyloid polymers, indicating the free energy of aggregates (A) is significantly lower than that for unfolded (U) and native (N) monomers at those(More)
Monomeric and aggregated states of an IgG1 antibody were characterized under acidic conditions as a function of solution pH (3.5-5.5). A combination of intrinsic/extrinsic fluorescence (FL), circular dichroism, calorimetry, chromatography, capillary electrophoresis, and laser light scattering were used to characterize unfolding, refolding, native colloidal(More)
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