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Updated: May 3, 2026
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Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy
Published on: September 12, 2019
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Nanoscale spatially resolved infrared spectra from single microdroplets
Thomas Müller1, Francesco Simone Ruggeri, Andrzej J Kulik
1Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK. tpjk2@cam.ac.uk.
Lab on a Chip
|February 13, 2014
Summary
This study presents a new method for infrared spectroscopy of single microdroplets, enabling the analysis of protein aggregation at the nanoscale. This technique resolves structural differences in aggregation-prone proteins like lysozyme.
Area of Science:
- Biophysical Chemistry
- Microfluidics
- Spectroscopy
Background:
- Droplet microfluidics enables numerous reactions in microcompartments.
- Spectroscopic characterization of species in microdroplets is challenging due to their small size.
Purpose of the Study:
- To develop a method for acquiring infrared spectra from single microdroplets.
- To analyze structural differences in aggregation-prone proteins at the single-droplet level.
Main Methods:
- Droplets generated using flow-focussing microfluidics.
- Droplets deposited in an array onto a ZnSe prism using a micro stamp.
- Infrared laser illumination and atomic force microscopy (AFM) for thermal expansion measurement.
Main Results:
- Successful acquisition of infrared spectra from single picolitre-volume microdroplets.
- Resolution of structural differences in the amide bands of monomeric and aggregated lysozyme.
- Demonstration of nanoscale resolution for spectroscopic analysis.
Conclusions:
- The developed method allows for detailed structural analysis of proteins in single microdroplets.
- This technique is valuable for studying protein aggregation and other molecular processes at the microscale.
- Advances spectroscopic capabilities for analyzing minute biological samples.
