Application Notes & White Papers
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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Common structural characterization methods such as FTIR and CD have known limitations in reproducibility and sensitivity which adversely increase the lowest level of quantitation (LOQ) achievable when measuring structural impurities and similarity. This application note will highlight the MMS system developed by RedShiftBio, a new protein characterization method which generates reproducible high resolution measurements. Demonstrated here, across a structural impurity range of 0–10%, are lower LOQ values compared to those possible using FTIR and CD.
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This whitepaper provides an overview of RedShiftBio’s Microfluidic Modulation Spectroscopy technology and the performance that can be achieved in protein characterization. Specifically the white paper presents significant increases in sensitivity and concentration range for determining protein similarity (fingerprinting), quantitation, protein secondary structure, and protein stability and aggregation through thermal and chemical denaturation methods.
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