Neutron reflectivity measurement of protein A-antibody complex at the solid-liquid interface.

ABSTRACT: Chromatography is a ubiquitous unit operation in the purification of biopharmaceuticals yet few studies have addressed the biophysical characterisation of proteins at the solution-resin interface. Chromatography and other adsorption and desorption processes have been shown to induce protein aggregation which is undesirable in biopharmaceutical products. In order to advance understanding of how adsorption processes might impact protein stability, neutron reflectivity was used to characterise the structure of adsorbed immunoglobulin G (IgG) on model surfaces. In the first model system, IgG was adsorbed directly to silica and demonstrated a side-on orientation with high surface contact. A maximum dimension of 60Å in the surface normal direction and high density surface coverage were observed

SUBMITTER: Mazzer AR 

PROVIDER: S-EPMC5408906 | biostudies-literature | 2017 May

REPOSITORIES: biostudies-literature