RedShiftBio Exhibits Solution for Formulation Development at Peptalk 2020
We are exhibiting at Peptalk in San Diego, CA (Jan 20-24, 2020). Come and see us at booth 506 to see the multi award-winning AQS3pro. Peptalk Protein Science Week is attended by the most influential in the biotherapeutics industry. If you are working in formulation development and require high quality data to discern differences in your sample, then visit RedShiftBio at booth 506 to learn more about our next-generation IR-based AQS3pro for secondary structure characterization.
Microfluidic Modulation Spectroscopy for Formulation Development
Our microfluidic modulation spectroscopy (MMS)-based AQS3pro leverages IR to enable you to see change in your proteins, fast. The AQS3pro directly addresses both the technical and commercial limitations of current secondary structure analysis technologies (FTIR, CD-UV etc). It provides unmatched dynamic range, increased sensitivity and multi sample walk away operation, all at low running costs while deploying small sample volumes.
We are presenting a poster at the conference with Pressure Biosciences. Come meet with the team to learn about how to use Microfluidic Modulation Spectroscopy (MMS) coupled with pressure-perturbation of proteins for biopharmaceutical formulations development.
High hydrostatic pressure is a thermodynamic driver causing unfolding of proteins orthogonal to the action of temperature or various chaotropic reagents. Pressure effects on protein conformation are explained by hydration of solvent-excluded cavities that are populated with solvent upon unfolding.
Infrared spectroscopy, along with circular dichroism and fluorescence, is a popular method for monitoring protein structure changes. Recently introduced Microfluidic Modulation Spectroscopy (MMS) represents a major advancement of infrared spectroscopy specifically developed to simplify protein structure analysis. Pressure effects on proteins is highly reproducible and can be controlled very precisely. Pressure perturbation approach coupled with MMS can be used to study stability of human immunoglobulins as a model system for formulations development of monoclonal antibody products and other biopharmaceuticals.
In this study we demonstrate that pressure unfolding of human immunoglobulins in specific chemical environments promotes quantitative conversion of parallel beta sheet structures to the anti-parallel beta structures, a characteristic indicator of amyloid protein aggregation. We explore pressure effects on aggregation kinetics in a series of co-solvents, chaotropes and popular stabilizing excipients. Pressure perturbation approach coupled with MMS can be used to study stability of human immunoglobulins as a model system for formulations development of monoclonal antibody products and other biopharmaceuticals.
The 2019 event will feature:
- 9 separate tracks
- 5 plenary keynotes
- 350+ scientific presentations
- 175+ posters
Come see us on booth 506 or pre-book a meeting with our team for during the conference.