AQS3™delta

Microfluidic Modulation Spectrometry (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, similarity, quantitation linearity, aggregation, and denaturation of proteins by analyzing the absorbance spectra and the high order structure (HOS). 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 using a RedShiftBio AQS3pro pre-production instrument.

RedShiftBio has developed a powerful new tool for protein structural analysis based on 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. The analyzer utilizes a tunable mid-infrared quantum cascade laser to generate an optical signal 1000X brighter than conventional sources used in FTIR spectroscopy.

The self-assembly of lysozyme to form amyloid fibrils is associated with systemic amyloidosis, a disease characterized by the presence of amyloid deposits in various organs of the body. The early events associated in the self-assembly of lysozyme are not well understood. In this work, 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. With heating at 60 ˚C, the β-turn content of the protein increases while its α-helical content decreases. This result suggests that the first structural transition in the self-assembly of human lysozyme is an α-helix to β-structure conformational rearrangement.