Learn more about Microfluidic Modulation Spectroscopy
Keep up-to-date on the latest developments in Microfluidic Modulation Spectroscopy (MMS), biophysical characterization and RedShiftBio by regularly visiting us here. On this page you will find our comprehensive resources, highlights from new papers and other interesting materials that will help you characterize proteins.
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Pressure-perturbation of protein secondary structure coupled with Microfluidic Modulation Spectroscopy – a powerful platform for biopharmaceutical formulations development
Vera Gross, Gary Smejkal, Nicole Cutri, Alexander Lazarev (Pressure Biosciences) Libo Wang, John Linnan, Matthew McGann, Jeffrey Zonderman, (RedShiftBio)
Microfluidic Modulation Spectroscopy (MMS) - a novel automated infrared (IR) spectroscopic tool for secondary structure analysis of biopharmaceuticals with high sensitivity and repeatability.
Dipanwita Batabyal, Harrison Lord, and Mats Wikström, Attribute Sciences, Amgen Inc, and Libo Wang, John Linnan and Jeffrey Zonderman,RedshiftBio
Presentations & webinars
The Department of Bioengineering University of Washington On Demand Webinar - Watch Now
How Microfluidic Modulation Spectroscopy (the AQS3pro) allows users to ‘see change’ in the secondary structure of proteins across a wide concentration range from 0.1 to over 200 mg/ml, and in the presence of excipients.
A team led by Brent Kendrick at KBI Biopharma, compare and assess FTIR and Circular Dichroism with Microfluidic Modulation Spectroscopy (RedShiftBio) for their ability to detect the presence and quantify the amount of the misfolded structure. in this Journal of Pharmaceutical Sciences paper
Biopharm International interviews scientists with experience of Microfluidic Modulation Spectroscopy for a round-table on how complex protein studies demand dynamic techniques. Visit page 18 to see what Immunogen, Janssen, Elion Labs and the University of Delaware have to say.
With the requirements of formulation development of biopharmaceuticals becoming more demanding, the evolution of analytical tools that can measure stability over a wide concentration range, in the presence of complex buffer systems is critical. Read this article in Drug Developmnet & Delivery to understand more about the role that MMS plays in formulation development.
A team led by researchers at the University of Washington has developed synthetic peptides that target and inhibit the small, toxic protein aggregates that are thought to trigger Alzheimer's disease
Whitepapers, Application & Technical Notes
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
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.
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).
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