Literature Resources

Whitepapers, Application & Technical Notes

whitepaper

MMS For Protein Therapeutic Drug Analysis - White Paper

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

white-paper-icon

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

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.

Analysis-of-Bovine-Serum

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

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).

Monoclonal-Antibody-Analysis

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

This note demonstrates that MMS enables quantitative analysis of monoclonal antibodies over a wide concentration range with high reproducibility and accuracy.