Maximizing the stability of a biopharmaceutical is not an easy task and therefore, a critical objective of any drug development program.
Aggregation and depletion of proteins and peptides in drug formulations is a major source of dosage form and storage instability. The presence of aggregates and sub-visible particles also compromises the safety and efficacy of the drug formulations and may lead to a series of problems during manufacturing, handling and post administration. As such the minimization of protein aggregation and chemical degradation is part of a de-risking strategy key to ensuring a smoother “developability” of a biopharmaceutical.
Aggregation is a complex phenomenon and it can proceed via different mechanism. Depending on the rate determining step aggregates can be formed via association of partially unfolded conformers or by interaction of the proteins in their native state. Moreover, partial unfolding can be caused by diverse factors, for example it can be caused by interaction with interphases or following chemical degradation (e.g. Oxidation).
It is well-known that recombinant human serum albumin has the ability to stabilize proteins in solution preventing adsorption, aggregation and oxidation. The stabilizing ability stems from some of the roles albumin performs in blood, such as a carrier of small hydrophobic entities, participation in the control of pH and osmotic pressure and affording the majority of the antioxidant capabilities present in blood.
Recombinant Human Albumin (rAlb) is therefore a promising stabilizer for hard-to-formulate biopharmaceuticals. In this webinar we will illustrate the use of Albumedix™ Recombumin®, a recombinant albumin product, as a stabilizing agent for model biopharmaceuticals, both peptides and monoclonal antibodies (mAbs) at high concentration, and elucidate on potential mechanisms.
Formation of aggregates and sub-visible particles during product storage is a major concern for formulation scientists due to the potential for loss, reduced efficacy, and increased immunogenicity of the product. Therefore, optimizing the stability of a therapeutic drug during final drug formulation, handling and storage is imperative to producing a safe final product with an appropriate shelf-life.
Albumedix will in this webinar share from our 30 years’ of expertise within this area, in an aim to bring valuable yet initially unstable drug candidates to market and create better quality of life for patients and their families.
Phil Morton
Science Director
Phil Morton is a Science Director heading up the Bioprocess Characterisation function within Albumedix R&D. He has 20+ years’ experience in the biopharmaceutical industry within process and product development.
His experience ranges from developing and transferring purification processes, to formulation development and characterisation of these processes and products. Phil holds a Ph.D. in Biochemical Eng. from Birmingham University and followed this with post-doctoral studies at Cambridge University.
Eleonora Cerasoli
Senior Scientist
Eleonora current focus is to study the stabilisation properties of Recombumin on an array of model systems. Previously she worked in the National Physical Laboratory on diverse topics such as protein aggregation, peptides biophysical characterisation and interaction with membranes.
Her background is biophysical chemistry (Chemistry degree, university of Rome), a PhD in Biochemistry on protein folding (Glasgow University) and post-doctoral experience in on peptide design (Prof. Woolfson Lab, now Bristol University).
- Key Areas for Developability Risk Assessment
- Protein Aggregation and Chemical Stability
- Productivity and Yield
- Safety in Biopharmaceuticals: Immunogenicity and Immunotoxicology
- Science Managers
- Heads of Research and Development
- Formulation Scientists
- Project Managers
