Abstract

Biopharmaceuticals or therapeutically relevant proteins have become one of the fastest growing parts of the pharmaceutical industry. These innovative molecules are much more complex than conventional drugs and their processing is much more demanding. Assessing, at a very early stage in the development process, the ease of manufacture (the manufacturability) would allow the candidates proteins to be ranked and thus help controlling the cost-effectiveness of new drugs. Our research project aims to identify critical properties of protein candidates allowing the prediction of their behaviour in large-scale bioprocesses. Our multidisciplinary approach combines computational analysis (Molecular Dynamics simulations), the pilot-scale production and the biophysical characterization of a set of Fragment antibody (Fab) mutants.This allowed the identification of regions of unstable structure helping to predict the stability of Fab candidates prior to experiments. Extensive aggregation kinetics were measured at a wide range of temperature, pH and ionic strength allowing the determination of a model for Fab aggregation and the development of a rapid micro-scale Fragment antibody aggregation screening method.

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