Structural analysis and mapping of individual protein complexes by infrared nanospectroscopy

Iban Amenabar, Simon Poly, Wiwat Nuansing, Elmar H. Hubrich, Alexander A. Govyadinov, Florian Huth, Roman Krutokhvostov, Lianbing Zhang, Mato Knez, Joachim Heberle, Alexander M. Bittner and Rainer Hillenbrand ()
Additional contact information
Iban Amenabar: CIC nanoGUNE Consolider
Simon Poly: CIC nanoGUNE Consolider
Wiwat Nuansing: CIC nanoGUNE Consolider
Elmar H. Hubrich: Experimental Molecular Biophysics, Freie Universität Berlin
Alexander A. Govyadinov: CIC nanoGUNE Consolider
Florian Huth: CIC nanoGUNE Consolider
Roman Krutokhvostov: CIC nanoGUNE Consolider
Lianbing Zhang: CIC nanoGUNE Consolider
Mato Knez: CIC nanoGUNE Consolider
Joachim Heberle: Experimental Molecular Biophysics, Freie Universität Berlin
Alexander M. Bittner: CIC nanoGUNE Consolider
Rainer Hillenbrand: CIC nanoGUNE Consolider

Nature Communications, 2013, vol. 4, issue 1, 1-9

Abstract: Abstract Mid-infrared spectroscopy is a widely used tool for material identification and secondary structure analysis in chemistry, biology and biochemistry. However, the diffraction limit prevents nanoscale protein studies. Here we introduce mapping of protein structure with 30 nm lateral resolution and sensitivity to individual protein complexes by Fourier transform infrared nanospectroscopy (nano-FTIR). We present local broadband spectra of one virus, ferritin complexes, purple membranes and insulin aggregates, which can be interpreted in terms of their α-helical and/or β-sheet structure. Applying nano-FTIR for studying insulin fibrils—a model system widely used in neurodegenerative disease research—we find clear evidence that 3-nm-thin amyloid-like fibrils contain a large amount of α-helical structure. This reveals the surprisingly high level of protein organization in the fibril’s periphery, which might explain why fibrils associate. We envision a wide application potential of nano-FTIR, including cellular receptor in vitro mapping and analysis of proteins within quaternary structures.

Date: 2013
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:4:y:2013:i:1:d:10.1038_ncomms3890

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DOI: 10.1038/ncomms3890

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