Application Notes & White Papers

Detection of Pressure-Induced Aggregation Using Microfluidic Modulation Spectroscopy (MMS)

April 8, 2021

Detection of Pressure-Induced 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. Application Note Introduction Protein aggregation is a recognized signal of instability and … “Detection of Pressure-Induced Aggregation Using Microfluidic Modulation Spectroscopy (MMS)”

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Using Microfluidic Modulation Spectroscopy to Determine the Structural Effect of pH on the Peptide Hormone Insulin

Using Microfluidic Modulation Spectroscopy to Determine the Structural Effect of pH on the Peptide Hormone Insulin

December 1, 2020

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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Detecting Protein Conformational Change Due to Ligand Binding and Stabilization Using MMS

Detecting Protein Conformational Change Due to Ligand Binding and Stabilization Using MMS

December 1, 2020

Ligand binding can affect the function of proteins and often causes conformational change in the protein target.

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Assessment of Quantitation Linearity for Bovine Serum Albumin Using MMS

Assessment of Quantitation Linearity for Bovine Serum Albumin Using MMS

December 1, 2020

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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Secondary Structure Analysis of NIST Monoclonal Antibody Reference Material 8671 by Microfluidic Modulation Spectroscopy

Secondary Structure Analysis of NIST Monoclonal Antibody Reference Material 8671 by Microfluidic Modulation Spectroscopy

October 1, 2020

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

Secondary Structure Determination using Microfluidic Modulation Spectroscopy in the Presence of DMSO

October 1, 2020

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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Monoclonal Antibody Analysis by Microfluidic Modulation Spectroscopy in a Complex Formulation Buffer (1 to 150 mg/mL)

March 1, 2019

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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Thermal Denaturation Analysis of Bovine Serum Albumin over Wide Concentration Range by Microfluidic Modulation Spectroscopy

January 1, 2019

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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Drug Development & Delivery: White paper on Protein Characterization Analytical Techniques

April 30, 2018

Today’s analytical techniques for protein characterization have deficiencies that hamper biopharmaceutical scientists in their mission to bring to market safer, more stable treatments for disease. Learn about a new analytical technique that addresses these shortcomings, allowing users to See Change™ in their proteins, not previously possible: Sensitivity to See Change More confidence in your analytical … “Drug Development & Delivery: White paper on Protein Characterization Analytical Techniques”

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Microfluidic Modulation Spectroscopy (MMS) Fills an Analytical Gap with a Lower LOQ for Measuring Protein Misfolds and Structural Similarity

January 1, 2018

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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