AQS3Pro enables more sensitive & reproducible Protein Secondary Structure analysis using MMS
When developing biotherapeutics, the ability to measure and characterise changes in the secondary structure of proteins is critical. Proteins in solution are prone to conformational change or instability as structural bonds are disrupted with thermal and chemical stresses in the local environment. Any structural change has the potential to compromise efficacy and trigger aggregation which can impact safety.
Conventional techniques such as FTIR and Circular Dichroism do not possess the adequate feature set for researchers to accurately assess changes in their proteins within the required conditions. The need for high sensitivity, a wide dynamic range, a simplified and automated workflow, and high repeatability is significant and, until now, has not been adequately provided.
The AQS3pro fills the gap for high sensitivity protein analysis with the novel IR technique called Microfluidic Modulation Spectroscopy (MMS).
The technique is purposely designed to directly address the limitations of current technologies and provide drift-free, background subtracted, high sensitivity measurements of the protein secondary structure. It is possible to measure protein similarity (fingerprinting), quantitation, higher order structure, protein stability, and aggregation through thermal and chemical denaturation methods using a walk-away automated platform.
The AQS3pro allows users to ‘see change’ in the secondary structure of proteins across a wide concentration range from 0.1mg/mL to over 200 mg/mL, and in the presence of excipients – the concentration range found across the full spectrum of drug development. Samples can be measured with minimal preparation and without dilution to generate data that is reliably representative of drug performance.
The AQS3™pro measures five key measurements—aggregation, quantitation, stability, similarity, structure to directly support protein characterisation throughout the biopharmaceutical development pipeline.
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