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Structural analysis and mapping of individual protein complexes by infrared nanospectroscopy
Open accessAbstract
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. Mid-infrared spectroscopy offers important chemical and structural information about biological samples but diffraction prevents nanoscale studies. Amenabar et al.demonstrate Fourier transform infrared nanospectroscopy for analysing the secondary structure of protein complexes with 30 nm spatial resolution.
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Cites
Fourier Transform Infrared Spectrometry
Griffiths, P. R., & de Haseth, J. A. (2007) · doi:10.1002/047010631x · Cited by 3,052
Examination of the secondary structure of proteins by deconvolved FTIR spectra
Byler, D. M., & Susi, H. (1986) · Biopolymers · doi:10.1002/bip.360250307 · Cited by 3,003
Three-dimensional model of purple membrane obtained by electron microscopy
Henderson, R., & Unwin, P. N. T. (1975) · Nature · doi:10.1038/257028a0 · Cited by 2,282
The Use and Misuse of FTIR Spectroscopy in the Determination of Protein Structure
Jackson, M., & Mantsch, H. H. (1995) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409239509085140 · Cited by 2,037
Oesterhelt, D., & Stoeckenius, W. (1974) · Methods in Enzymology · doi:10.1016/0076-6879(74)31072-5 · Cited by 1,687
Nanoscale chemical analysis by tip-enhanced Raman spectroscopy
Stöckle, R. M., Suh, Y. D., Deckert, V., & Zenobi, R. (2000) · Chemical Physics Letters · doi:10.1016/s0009-2614(99)01451-7 · Cited by 1,606
Protein−Nanoparticle Interactions: Opportunities and Challenges
Mahmoudi, M., Lynch, I., Ejtehadi, M. R., Monopoli, M. P., Bombelli, F. B., & Laurent, S. (2011) · Chemical Reviews · doi:10.1021/cr100440g · Cited by 1,426
High-Resolution Near-Field Raman Microscopy of Single-Walled Carbon Nanotubes
Hartschuh, A., Sánchez, E. J., Xie, X., & Novotný, L. (2003) · Physical Review Letters · doi:10.1103/physrevlett.90.095503 · Cited by 870
The protofilament structure of insulin amyloid fibrils
Jiménez, J. L., Nettleton, E. J., Bouchard, M., Robinson, C. V., Dobson, C. M., & Saibil, H. R. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.142459399 · Cited by 834
Multitargeting by curcumin as revealed by molecular interaction studies
Gupta, S. C., Prasad, S., Kim, J. H., Patchva, S., Webb, L. J., Priyadarsini, I. K., & Aggarwal, B. B. (2011) · Natural Product Reports · doi:10.1039/c1np00051a · Cited by 669
Nano-FTIR Absorption Spectroscopy of Molecular Fingerprints at 20 nm Spatial Resolution
Huth, F., Govyadinov, A., Amarie, S., Nuansing, W., Keilmann, F., & Hillenbrand, R. (2012) · Nano Letters · doi:10.1021/nl301159v · Cited by 633
Self-citationVenyaminov, S. Y., & Kalnin, N. N. (1990) · Biopolymers · doi:10.1002/bip.360301309 · Cited by 590
Pseudoheterodyne detection for background-free near-field spectroscopy
Ocelic, N., Huber, A., & Hillenbrand, R. (2006) · Applied Physics Letters · doi:10.1063/1.2348781 · Cited by 579
Self-citationFunctional waters in intraprotein proton transfer monitored by FTIR difference spectroscopy
Garczarek, F., & Gerwert, K. (2006) · Nature · doi:10.1038/nature04231 · Cited by 531
Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy
Bouchard, M., Zurdo, J., Nettleton, E. J., Dobson, C. M., & Robinson, C. V. (2000) · Protein Science · doi:10.1110/ps.9.10.1960 · Cited by 482
Correlation of structural elements and infectivity of the HET-s prion
Ritter, C., Maddelein, M.-L., Siemer, A. B., Lührs, T., Ernst, M., Meier, B. H., Saupe, S. J., & Riek, R. (2005) · Nature · doi:10.1038/nature03793 · Cited by 437
Imaging of colorectal adenocarcinoma using FT-IR microspectroscopy and cluster analysis
Lasch, P., Haensch, W., Naumann, D., & Diem, M. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2003.12.006 · Cited by 405
Tip-Enhanced Coherent Anti-Stokes Raman Scattering for Vibrational Nanoimaging
Ichimura, T., Hayazawa, N., Hashimoto, M., Inouye, Y., & Kawata, S. (2004) · Physical Review Letters · doi:10.1103/physrevlett.92.220801 · Cited by 405
Molecular basis for insulin fibril assembly
Ivanova, M. I., Sievers, S. A., Sawaya, M. R., Wall, J. S., & Eisenberg, D. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0910080106 · Cited by 393
Infrared and Raman Spectroscopic Imaging
(2009) · Wiley eBooks · doi:10.1002/9783527628230 · Cited by 333
Khurana, R., Ionescu-Zanetti, C., Pope, M., Li, J., Nielson, L., Ramírez-Alvarado, M., Regan, L., Fink, A. L., & Carter, S. A. (2003) · Biophysical Journal · doi:10.1016/s0006-3495(03)74550-0 · Cited by 309
Infrared-spectroscopic nanoimaging with a thermal source
Huth, F., Schnell, M., Wittborn, J., Ocelic, N., & Hillenbrand, R. (2011) · Nature Materials · doi:10.1038/nmat3006 · Cited by 306
Self-citationInfrared Spectroscopic Mapping of Single Nanoparticles and Viruses at Nanoscale Resolution
Brehm, M., Taubner, T., Hillenbrand, R., & Keilmann, F. (2006) · Nano Letters · doi:10.1021/nl0610836 · Cited by 250
Self-citationPolarized infrared spectroscopy of oriented purple membrane
Rothschild, K. J., & Clark, N. A. (1979) · Biophysical Journal · doi:10.1016/s0006-3495(79)85317-5 · Cited by 237
Govyadinov, A. A., Amenabar, I., Huth, F., Carney, P. S., & Hillenbrand, R. (2013) · The Journal of Physical Chemistry Letters · doi:10.1021/jz400453r · Cited by 211
Self-citationStructure and Composition of Insulin Fibril Surfaces Probed by TERS
Kurouski, D., Deckert-Gaudig, T., Deckert, V., & Lednev, I. K. (2012) · Journal of the American Chemical Society · doi:10.1021/ja303263y · Cited by 172
Ferritins for chemistry and for life
Theil, E. C., Behera, R. K., & Tosha, T. (2013) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2012.05.013 · Cited by 158
Guo, S., & Akhremitchev, B. B. (2006) · Biomacromolecules · doi:10.1021/bm0600724 · Cited by 153
Signatures of β-sheet secondary structures in linear and two-dimensional infrared spectroscopy
Cheatum, C. M., Tokmakoff, A., & Knoester, J. (2004) · The Journal of Chemical Physics · doi:10.1063/1.1689637 · Cited by 145
Jiang, X., Zaitseva, E., Schmidt, M., Siebert, F., Engelhard, M., Schlesinger, R., Ataka, K., Vogel, R. F., & Heberle, J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0802289105 · Cited by 140
Self-citationNano-FTIR chemical mapping of minerals in biological materials
Amarie, S., Zaslansky, P., Kajihara, Y., Griesshaber, E., Schmahl, W. W., & Keilmann, F. (2012) · Beilstein Journal of Nanotechnology · doi:10.3762/bjnano.3.35 · Cited by 135
Ge, P., & Zhou, Z. H. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1018104108 · Cited by 127
Ataka, K., Kottke, T., & Heberle, J. (2010) · Angewandte Chemie International Edition · doi:10.1002/anie.200907114 · Cited by 117
Self-citationCaine, S., Heraud, P., Tobin, M. J., McNaughton, D., & Bernard, C. C. A. (2011) · NeuroImage · doi:10.1016/j.neuroimage.2011.11.033 · Cited by 115
Keilmann, F., & Amarie, S. (2012) · Journal of Infrared Millimeter and Terahertz Waves · doi:10.1007/s10762-012-9894-x · Cited by 106
Nano‐imaging through tip‐enhanced Raman spectroscopy: Stepping beyond the classical limits
Verma, P., Ichimura, T., Yano, T., Saito, Y., & Kawata, S. (2009) · Laser & Photonics Review · doi:10.1002/lpor.200910039 · Cited by 75
New Insights into the Self-Assembly of Insulin Amyloid Fibrils: An H−D Exchange FT-IR Study
Dzwolak, W., Loksztejn, A., & Smirnovas, V. (2006) · Biochemistry · doi:10.1021/bi060341a · Cited by 66
Tip-enhanced Raman scattering (TERS) and high-resolution bio nano-analysis—a comparison
Deckert‐Gaudig, T., & Deckert, V. (2010) · Physical Chemistry Chemical Physics · doi:10.1039/c003316b · Cited by 60
Paulite, M., Fakhraai, Z., Li, I. T. S., et al. (2011) · Journal of the American Chemical Society · doi:10.1021/ja109316p · Cited by 57
Höppener, C., Siebrasse, J. P., Peters, R., Kubitscheck, U., & Naber, A. (2005) · Biophysical Journal · doi:10.1529/biophysj.104.051458 · Cited by 54
Biomimetic collagen/apatite coating formation on Ti6Al4V substrates
Xia, Z., Yu, X., & Wei, M. (2011) · Journal of Biomedical Materials Research Part B Applied Biomaterials · doi:10.1002/jbm.b.31970 · Cited by 53
Selivanova, O. M., & Galzitskaya, O. V. (2012) · Biochemistry (Moscow) · doi:10.1134/s0006297912110028 · Cited by 42
Nanoscale depth resolution in scanning near-field infrared microscopy
Wollny, G., Bründermann, E., Arsov, Z., Quaroni, L. G., & Havenith, M. (2008) · Optics Express · doi:10.1364/oe.16.007453 · Cited by 38
Super-resolved FT-IR spectroscopy: Strategies, challenges, and opportunities for membrane biophysics
Li, J. J., & Yip, C. M. (2013) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2013.02.013 · Cited by 16
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Etezadi, D., Warner IV, J. B., Ruggeri, F. S., Dietler, G., Lashuel, H. A., & Altug, H. (2017) · Light: Science & Applications · doi:10.1038/lsa.2017.29 · Cited by 137
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Metadata
- Authors
- Amenabar, I., Poly, S., Nuansing, W., Hubrich, E. H., Govyadinov, A. A., Huth, F., Krutokhvostov, R., Zhang, L., Knez, M., Heberle, J., Bittner, A. M., & Hillenbrand, R.
- Venue
- Nature Communications
- Published
- 2013-12-04
- Volume
- 4
- Issue
- 1
- Pages
- 2890-2890
- ISSN
- 2041-1723 (ISSN-L)
- OpenAlex
- W2009783036
- Cited by
- 403
- References
- 44
- FWCI
- 11.20
- Type
- journal article
- Language
- en
- Open access
- hybrid
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