Using Microfluidic Modulation Spectroscopy for Peptide Quality Control

Abstract

Peptides are an increasingly popular and attractive therapeutic agent due to their specificity, versatility, and manufacturability. In this study, two lots of the same immunogenic peptide produced using different synthesis processes were indistinguishable by standard biophysical techniques but showed different efficacy in animal models.

Using Aurora TX, MMS revealed that while native structures in water were similar, both peptides exhibited aggregation in PBS with increased beta-sheet content. Importantly, the Process 1 peptide retained more native turn structure and less unordered structure compared to Process 2 under stress conditions.

These findings suggest that structural differences in physiological-like buffers correlate with potency and demonstrate MMS as a powerful tool for peptide quality control and process development.