Application Notes & White Papers
It was determined that many of the Bovine Serum Albumin (BSA) reference candidates did not exhibit acceptable activity after inclusion into the final product though all purchased samples shared the same name and identification. The inconsistency in activity causes delays, increases cost of manufacture, and adds an element of variability. Current in-house biophysical techniques fail … “Biosimilar Structural Comparison of Commercially Sourced Reference Standards by MMS Rapidly Detects Subtle but Critical Differences to Correctly Predict Activity for Use in an ELISA Product”
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Biosimilar Comparison and Accelerated Stability Predictions Based on <2% Secondary Structure Differences Using Microfluidic Modulation Spectroscopy (MMS) Biosimilar structure analysis and stability predictions require instrumentation sensitive enough to detect critical small changes in secondary structure. The ability to see these structural differences between engineered biosimilars and their innovator molecules is vital to ensure successful drug approval. Biosimilar structure analysis and stability predictions … “Biosimilar Comparison and Accelerated Stability Predictions Based on <2% Secondary Structure Differences Using Microfluidic Modulation Spectroscopy (MMS)"
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Detection of Pressure-Induced Protein Aggregation Using MicrofluidicModulation Spectroscopy (MMS) The ability to detect protein aggregation is important at all stages of drug development. Early detection of aggregation is most desirable to inform development decisions since aggregation can negatively affect the functionality of a protein. Pressure-Induced Protein Aggregation Detection Protein aggregation is a recognized signal of … “Detection of Pressure-Induced Protein Aggregation Using Microfluidic Modulation Spectroscopy (MMS)”
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Secondary structure characterization is an essential part of drug development, however, the tools for measuring secondary structure of small proteins and peptides are limited.
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Ligand binding can affect the function of proteins and often causes conformational change in the protein target.
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Microfluidic Modulation Spectroscopy (MMS) is a revolutionary new technology capable of highly sensitive and reproducible measurements of protein secondary structure using IR absorbance in the Amide I band (1700-1600 cm-1).
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In 2016 the National Institute of Standards and Technology (NIST) made NISTmAb Reference Material (RM) 8671 commercially available for the evaluation of methods used to characterize the structure of monoclonal antibodies.
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Secondary Structure Determination using Microfluidic Modulation Spectroscopy in the Presence of DMSO
Characterizing biologic drug products is crucial in drug development and the presence of organic solvents and optically active excipients typically hinders traditional characterization techniques.
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This note demonstrates that MMS enables quantitative analysis of monoclonal antibodies over a wide concentration range with high reproducibility and accuracy.
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In this note, MMS was used to study the heat-induced thermal denaturation of BSA. The results show replicate measurements are very reproducible (99% similarity), and that MMS provides accurate secondary structure measurements for protein samples over a wide concentration range (1 to 100 mg/mL).
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