Protein-protein interactions, viscosity and injectability in multi protein co-formulations comprising Bevacizumab and recombinant HSA
It is well-known that recombinant HSA (rHSA) has the ability to stabilize proteins in in solution preventing protein adsorption, protein aggregation and protein oxidation. At low protein drug concentrations (< 1mg/mL) the mechanism of action is relatively well understood and the beneficial effect is expected to act through coating of hydrophobic and hydrophilic surfaces on the primary packaging […]
An atomic force microscopy based method for biopharmaceutical stability determination
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Nanosight
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Malvern Instruments
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GE Healthcare
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Avacta
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Susanne Jörg
Novartis Pharma AG, Switzerland – susanne.joerg@novartis.com Special aspects in the pharmaceutical development of protein formats beyond mAbs In the past decades, monoclonal antibodies have become the fastest growing area of biopharmaceutical industry. Currently, alternative protein formats – such as FAbs, scFvs, nanobodies, etc – are under development. These new antibody and therapeutic protein formats come along with […]
Dr. Leonardo Borras
Alcon Labs (Novartis company) – leonardo.borras@alconlabs.com The Importance of Early Biophysical Characterization of Antibodies in the Lead Selection Process A critical aspect of the antibody lead selection process is assessing and understanding the biophysical properties of antibody lead candidates. An early characterization helps to reduce or eliminate development issues while allowing for ideal lead selection. We have […]
Dr. Leonardo Borras
Alcon Labs (Novartis company) – leonardo.borras@alconlabs.com The Importance of Early Biophysical Characterization of Antibodies in the Lead Selection Process A critical aspect of the antibody lead selection process is assessing and understanding the biophysical properties of antibody lead candidates. An early characterization helps to reduce or eliminate development issues while allowing for ideal lead selection. We have […]
Professor Michele Vendruscolo
Cambridge University – mv245@cam.ac.uk Sequence-based prediction of protein solubility As increasing evidence indicates that the sequences of proteins encode not just their folding but also their solubility and aggregation [1,2], there is great interest in identifying the amino acid code responsible for the maintenance of solubility. We have been developing computational methods to predict different aspects of […]