Demonstration video

Benefits

Key features of Aurora TX include:

• Ultra-sensitive and highly reproducible structural measurements
• Wide applicability across many therapeutic modalities
• 50uL of sample at 0.1mg/mL is all you need for highly reproducible data
• Thermal ramping capability for controlled temperature stress/stability assessments
• Walk-away automation with multiple measurements in a single analysis
• Robust delta software for simplified data collection and interpretation
• New, streamlined optional buffer station that enhances throughput by integrating up to 8 buffers directly into the system during analysis

Applications

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.

POSTER : MMS EVALUATION OF HOS FOR IGG SAMPLES SPIKED WITH BSA