The therapeutic and ultimately the commercial success of a protein-based drug depends upon the ability to produce a formulation with an adequate stability profile. The mechanisms of protein instability are complex and typically multiple excipients are required to address factors such as aggregation, oxidation and nonspecific adsorption during protein formulation.
"We are proud to present our latest, breakthrough research on recombinant human albumin and share our invaluable knowledge with other industry experts", comments Dermot Pearson, marketing director at Novozymes Biopharma. "As a leader in biomanufacturing and process development, we continue to perform studies designed to demonstrate how animal-free rAlbumin can help the industry optimize drug formulation, development and delivery."
The new poster, entitled "Recombinant Human Albumin: A Multifunctional Excipient for the Stabilisation of Therapeutic Protein Formulations", demonstrates the potential for recombinant human albumin (rAlbumin) to act as a multifunctional stabilisation excipient for protein and peptide formulations. The poster describes the study undertaken to investigate the stability of the rAlbumin with respect to pH and temperature to assess the suitability of this molecule for incorporation into protein formulations.
"We are proud to present our latest, breakthrough research on recombinant human albumin and share our invaluable knowledge with other industry experts", comments Dermot Pearson, marketing director at Novozymes Biopharma. "As a leader in biomanufacturing and process development, we continue to perform studies designed to demonstrate how animal-free rAlbumin can help the industry optimize drug formulation, development and delivery."
The new poster, entitled "Recombinant Human Albumin: A Multifunctional Excipient for the Stabilisation of Therapeutic Protein Formulations", demonstrates the potential for recombinant human albumin (rAlbumin) to act as a multifunctional stabilisation excipient for protein and peptide formulations. The poster describes the study undertaken to investigate the stability of the rAlbumin with respect to pH and temperature to assess the suitability of this molecule for incorporation into protein formulations.
The study results indicate that rAlbumin is a multifunctional excipient, protecting protein-based active ingredients against aggregation, oxidation
and non-specific binding in solution. The multifunctional nature of rAlbumin may lead to opportunities to explore simpler protein formulations with reduced numbers of excipients. Additionally, the stability of the molecule reveals its potential to be used under a wide range of formulation conditions.
and non-specific binding in solution. The multifunctional nature of rAlbumin may lead to opportunities to explore simpler protein formulations with reduced numbers of excipients. Additionally, the stability of the molecule reveals its potential to be used under a wide range of formulation conditions.
