Sensing Protein Structural Transitions with Microfluidic Modulation Infrared Spectroscopy

Abstract

This new publication from Baylor College of Medicine describes how the AuroraTX instrument, powered by our Microfluidic Modulation Spectroscopy (MMS), was used to characterize the structure of Intrinsically Disordered Proteins (IDPs) to monitor their transitions.

It works by using an alternating-flow design to subtract buffer backgrounds from the protein signals in real time, yielding clear amide I spectra from minimal sample volumes without the need for deuterated solvents. This high-sensitivity approach allows for the quantitative analysis of protein secondary structures, enabling the detection of subtle shifts in transient conformers and the monitoring of aggregation pathways in both folded and disordered systems. The technique's compatibility with native buffers and rapid acquisition makes it well-suited for probing dynamic ensembles and mapping aggregation-related diseases.  

Quoting the author's highlight of MMS's benefits: "MMS’s minimal sample requirements and label-free operation further make it an ideal platform for high-throughput screening of modulators that stabilize or disrupt specific structural ensembles. Its ability to probe dynamic conformational landscapes under varied environmental and post-translational modifications positions MMS as a powerful tool for the future of drug discovery."

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