RedShiftBio European Product Launch at PEGS EU 2018 Booth #04

Following the successful introduction of the AQS3TMpro in the US, RedShiftBio is excited to announce the unveiling of its IR-based instrument at PEGS EU. The instrument is powered by a new technology called Microfluidic Modulation Spectroscopy, allowing you to see change in protein secondary structure that was not previously possible. Driven by the industry-leading AQS3delta Analytical Software package, it streamlines and simplifies 5 key measurements:

Aggregation | Quantitation | Stability | Structure | Similarity

Come meet with us during the conference on booth #04 or at our poster:

Poster Session C (Thursday) C45: ‘Microfluidic Modulation Spectroscopy Analysis of a Monoclonal Antibody at Different Concentrations’

  • 1Libo Wang, 2Ioannis A. Papayannopoulos, 2Shannon Renn-Bingham, and 1Jeffery Zonderman
  • 1RedShift BioAnalytics, Inc., Burlington, Massachusetts
  • 2Celldex Therapeutics, Inc., Fall River, Massachusetts

Enter your details to book a meeting.

Microfluidic Modulation Spectroscopy (MMS) is a novel protein characterization technique that combines a microfluidic cell and a tunable mid-IR quantum cascade laser source to assess the comparability, stability, similarity, quantitation, linearity, denaturation and aggregation of proteins by analyzing the absorbance spectra and their correlation to higher order structures HOS). To evaluate the data quality and performance of MMS, an antibody sample, formulated at relatively high concentration, was analyzed using MMS on a RedShiftBio preproduction AQS3TMpro instrument at different concentrations from 1 mg/mL to 150 mg/mL. The differential absorbance (diffAU) spectra across the amide-I band were measured, the absolute absorbance (absAU) spectra were derived, the Area of Overlap (AO) plots and the similarity of the samples were compared, and the HOS was elucidated. Our results show that the diffAU spectra of replicates for each sample are very closely matched indicating high repeatability and accuracy of the measurements. Whereas the maximum diffAU signal versus protein concentration data fits a straight line with an R2 value of 0.999 displaying great quantitation linearity of measurements at concentrations from 1 mg/mL to 150 mg/mL. The absAU spectra of the mAb samples at concentrations from 5 mg/mL to 150 mg/mL overlay very well, suggesting a common secondary structure profile of these samples; while that of the 1 mg/mL sample show some slight differences but are still very comparable. When comparing the AO plots to the mean AO plot of the 5 mg/mL sample replicates, the similarity is 98.2-98.7% for 1 mg/mL sample and 99.2-99.8% for all the other samples, showing that the MMS tool offers very reproducible measurements at a wide range of concentrations. In addition, the HOS analysis yields consistent secondary structure estimations for these samples, i.e. 59-61% beta sheet structure, 28-29% turn structure and very small amounts of alpha-helix and unordered structures. No dilution of high concentration samples is required for MMS measurements and there are no interferences from optically active components in formulation buffers. Our results show that MMS is a powerful protein characterization technique providing comparability, similarity, quantitation linearity and HOS information of protein samples with high sensitivity and accuracy.