Comparability, Similarity, Linearity and High Order Structure Analysis of an IgG1 Sample by Microfluidic Modulation Spectroscopy
To evaluate the data quality and performance of MMS, an IgG1 sample was analyzed at different concentrations ranging from 0.1 mg/mL to 12.3 mg/mL. Our data shows that MMS has proved to be a powerful protein characterization technique to provide comparability, similarity, quantitation linearity and HOS measurements of protein samples.
Microfluidic Modulation Spectroscopy of a Biotherapeutic at Low to High Concentrations without Interference from Formulation Excipients. (Libo Wang and Jeffrey Zonderman, RedShiftBio, and Ioannis A. Papayannopoulos and Shannon Renn-Bingham, Celldex)
Our data indicates that MMS is a powerful automated protein characterization tool for secondary structure assessment of biopharmaceuticals with high repeatability, accuracy and sensitivity, applicable to wide concentration ranges and buffers with various excipients, enabling structural characterization not achievable using traditional FTIR and far-UV CD methods.
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)
To assess the sensitivity of MMS, we first analyzed a monoclonal antibody (mAb) sample at low and high concentrations and compared the data to the traditional FTIR data. We also ran a BiTE sample (Bispecific T cell Engager) to test sensitivity for a different modality at low concentrations . The high similarity scores of both the samples at low concentrations indicates the high accuracy and sensitivity of this MMS Method.
HOS Study for IgG Samples Spiked with Different Amount of BSA by MMS (Libo Wang, RedShiftBio & Brent Kendrick, Elion Labs)
To evaluate the sensitivity of MMS to detect small differences in secondary structure, absorbance spectra are analyzed for protein samples containing BSA spiked into IgG. Results show that MMS is a powerful technique for the measurement and analysis of protein secondary structure and provides HOS data with high sensitivity and accuracy.
Microfluidic Modulation Spectroscopy Analysis of a Monoclonal Antibody at Different Concentrations ( Libo Wang RedShiftBio, Ioannis A. Papayannopoulos Celldex )
Thermal Denaturation Analysis of Bovine Serum Albumin by Microfluidic Modulation Spectroscopy (Lucy Liu, Pfizer)
MMS, a novel mid-IR technique, was used to monitor the thermal denaturation of Bovine Serum Albumin (BSA). Results show that MMS is a powerful technique for the measurement and analysis of protein secondary structure in samples over the wide concentration range of protein concentrations, up to 100 mg/mL.
Structural Characterization of the Insulin-Degrading Enzyme by Microfluidic Modulation Spectroscopy (Valerie Ivancic, Clark University & Libo Wang, RedShiftBio)
We used a new bioanalytical technique called Microfluidic Modulation Spectroscopy to directly probe the backbone structure of IDE in the absence and presence of ATP and insulin. Together, our results show that the interaction of ATP with IDE is localized to sidechains but the interaction of insulin with IDE leads to a perturbation in the backbone structure of the enzyme.
Repeatability , Concentration Linearity and High Order Structure Analysis of an IgG1 Sample by Microfluidic Modulation Spectroscopy (MMS) (Libo Wang, RedShiftBio & Lucy Liu, Pfizer)
To evaluate the data quality and performance of MMS, an IgG1 sample was analyzed at different concentrations ranging from 0.1 mg/mL to 12.3 mg/mL. MMS has proved to be a powerful protein characterization technique to provide comparability, similarity, quantitation linearity and HOS measurements of protein samples.
Early Events in Amyloid Formation by Lysozyme Detected by Microfluidic Modulation Spectroscopy (Quichen Zheng, Clark University & Libo Wang, RedShiftBio)
We used Microfluidic Modulation Spectroscopy (MMS) to characterize the early events in the self-assembly of human lysozyme. Through MMS, we were able to probe the mid-IR absorption band of the protein which is sensitive to both α-helix and β-structure. Results suggest that the first structural transition in the self-assembly of human lysozyme is an α-helix to β-structure conformational rearrangement.
Enhanced Protein Structural Characterization using MMS (Eugene Ma, RedShiftBio)
Introduction to Microfluidic Modulation Spectroscopy (MMS). This technology shows significant increases in sensitivity, dynamic range, accuracy and utility for determination of protein secondary structure, quantitation, similarity, stability and aggregation.