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Structural analysis and mapping of individual protein complexes by infrared nanospectroscopy

Author

Listed:
  • 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
    Neaspec GmbH)

  • Roman Krutokhvostov

    (CIC nanoGUNE Consolider)

  • Lianbing Zhang

    (CIC nanoGUNE Consolider)

  • Mato Knez

    (CIC nanoGUNE Consolider
    IKERBASQUE, Basque Foundation for Science)

  • Joachim Heberle

    (Experimental Molecular Biophysics, Freie Universität Berlin)

  • Alexander M. Bittner

    (CIC nanoGUNE Consolider
    IKERBASQUE, Basque Foundation for Science)

  • Rainer Hillenbrand

    (CIC nanoGUNE Consolider
    IKERBASQUE, Basque Foundation for Science)

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.

Suggested Citation

  • 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 & Ra, 2013. "Structural analysis and mapping of individual protein complexes by infrared nanospectroscopy," Nature Communications, Nature, vol. 4(1), pages 1-9, December.
    • Handle: RePEc:nat:natcom:v:4:y:2013:i:1:d:10.1038_ncomms3890
    DOI: 10.1038/ncomms3890
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    Cited by:

    1. Xuezhi Ma & Qiushi Liu & Ning Yu & Da Xu & Sanggon Kim & Zebin Liu & Kaili Jiang & Bryan M. Wong & Ruoxue Yan & Ming Liu, 2021. "6 nm super-resolution optical transmission and scattering spectroscopic imaging of carbon nanotubes using a nanometer-scale white light source," Nature Communications, Nature, vol. 12(1), pages 1-7, December.
    2. Borislav Hinkov & Florian Pilat & Laurin Lux & Patricia L. Souza & Mauro David & Andreas Schwaighofer & Daniela Ristanić & Benedikt Schwarz & Hermann Detz & Aaron M. Andrews & Bernhard Lendl & Gottfri, 2022. "A mid-infrared lab-on-a-chip for dynamic reaction monitoring," Nature Communications, Nature, vol. 13(1), pages 1-10, December.

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