AURORA TX

POSTER 1: MMS Evaluation of HOS for IGG samples spiked with BSA

POSTER 2: Structural Characterization and Comparison of Temperature and Pressure Stress on a Protein Library Across pH and Concentration Using Microfluidic Modulation Spectroscopy

KEY INSIGHTS

Secondary structure and thermal ramping capability
Characterise the structure of a wide range of biomolecules including RNA, LNPs, proteins, peptides, antibodies, ADCs, and AAVs by measuring change in stability due to buffer/pH/formulation, stress, point mutations, binding, and storage time/conditions.Thermal ramping applies stress in a repeatable and automated fashion to induce structural change and guide decision-making and candidate ranking, saving valuable R&D time.

Aggregation – This is a common indicator of protein instability, which can result in a therapeutic product being unfit for launch. MMS is one of the only techniques which can directly monitor the formation of aggregates due to its ability to measure intermolecular beta-sheet structures.

Quantitation of protein concentration – The structure and behavior of proteins in solution can be a function of their concentration, therefore the ability to accurately quantify protein concentration allows better comparison between different proteins and formulations. MMS’s high resolution (<0.001 cm-1) and low stray light susceptibility increases the linear concentration range for the measurement by more than 2 orders of magnitude. With a minimum measurable concentration of less than 10 μg/mL and an upper limit of greater than 200 mg/mL, this technique offers a significant improvement over conventional absorbance-based assays.

Protein Higher Order Structure (HOS) – During manufacturing, biopharmaceutical proteins may undergo conformational changes which can alter their secondary structure and therefore their function. MMS has the ability to detect these changes with great sensitivity, in the formulation buffer and at the concentration of interest, without the need for dilution or deuteration. MMS offers detailed information on which structural motifs in the protein molecule are changing, to help guide the development of more stable protein molecules and formulations.

Protein Stability – Measuring how stable a protein is to thermal or chemical exposure during manufacturing and storage is critical. Structural changes can lead to decreases in potency, degradation of the product, and increases in impurities and aggregates which can be extremely harmful. MMS technology enables the accurate assessment of the stability of the protein throughout the entire formulation, development, and manufacturing process, reducing risks and enabling control strategies for each critical quality attribute (CQA).

Biosimilarity – Along with functional comparisons, measurement and analysis of the structural similarity between proteins is an effective method of demonstrating bioequivalence. MMS measures protein secondary structure, reveals very small conformation differences between different proteins, and provides information as to where those differences occur. These capabilities make MMS a powerful tool in the analysis and development of biosimilars.

What technology does the Aurora TX use to characterise biomolecules?

The Aurora TX is powered by Microfluidic Modulation Spectroscopy (MMS), which combines a quantum cascade laser, a microfluidic flow cell, and automated software. MMS generates a high-resolution differential absorbance spectrum across the Amide I region (1600-1700 cm-1), delivering 30x higher sensitivity than FTIR and 5x higher sensitivity than circular dichroism, with real-time background subtraction and reproducibility exceeding 98%.

What types of biomolecules can the Aurora TX characterise?

The Aurora TX characterises a broad range of biomolecules including proteins, peptides, monoclonal antibodies (mAbs), antibody-drug conjugates (ADCs), adeno-associated viruses (AAVs), mRNA, RNA, lipid nanoparticles (LNPs), intrinsically disordered proteins (IDPs), biosimilars, and nucleic acids — all from a single 50 uL drop of sample in native buffer conditions.

How does the Aurora TX assess biomolecule stability using thermal ramping?

The Aurora TX integrates thermal ramping to conduct controlled temperature stress assessments of biomolecule structure. As temperature increases, the system continuously measures secondary structure changes, enabling determination of thermal stability profiles and detection of structural transitions caused by heat stress. This allows researchers to evaluate the effects of buffer, pH, formulation, mutations, binding, or storage conditions on stability.

What sample preparation does the Aurora TX require?

The Aurora TX requires just 50 uL of sample per measurement and operates directly in complex buffer formulations without dilution or buffer exchange. The concentration range spans from 0.1 mg/mL to over 200 mg/mL. An optional buffer station can integrate up to 8 buffers into the system for automated buffer comparisons.

Can the Aurora TX detect protein aggregation and higher-order structure changes?

Yes. The Aurora TX detects intermolecular beta-sheet structures that are characteristic of protein aggregation, as well as broader higher-order structure (HOS) changes. It can also quantify protein concentration in the range of 10 ug/mL to over 200 mg/mL from the same measurement, making it a multi-parameter characterisation platform in a single analysis run.

Can the Aurora TX be used for RNA and lipid nanoparticle (LNP) characterisation?

Yes. The Aurora TX characterises RNA structure and measures RNA-to-LNP ratios, which is relevant for mRNA therapeutic development. The system’s MMS technology operates across the full range of nucleic acid and lipid formulations, enabling structural characterisation of LNP-encapsulated mRNA as well as free RNA.

How automated is the Aurora TX workflow?

The Aurora TX is fully automated and designed for walk-away operation. The Delta software provides an uncomplicated approach to data interpretation without requiring spectroscopy expertise. Multiple measurements can be run per analysis cycle, and the 96-well plate format supports batched sample processing, making it suitable for both development and quality control environments.

Can I have a demonstration or free trial of the Aurora TX?

Yes, if a system is available. Contact us for a booking. We can arrange a personalised demo and test your samples within our lab facility in Sydney. Onsite free trials are also available. Contact us or complete a request a demo form to get started.