Do carbon nanotubes inhibit or promote amyloid fibrils formation?
Abstract
Objectives: The purpose of the work was to study the effect of carbon nanotubes on the formation of fibril structures in lysozyme at room temperature under different pH values.
Materials and methods: For the preparation of the samples, hen egg-white lysozyme protein (HEWL, Fluka), as well as single-walled (SWCNT, Sigma-Aldrich) and multi-walled (MWCNT, OOO TM “Spetsmash”, Kyiv, Ukraine) carbon nanotubes were used. Used techniques: IR-Fourier Absorption Spectroscopy; confocal microscopy.
Results: In this paper, the study of molecular mechanisms of interaction of lysozyme with carbon nanotubes by vibrational spectroscopy was carried out and a conformational analysis of the formed complexes was performed. It is shown that carbon nanotubes can affect the structure of lysozyme even at room temperature and normal pH values, as evidenced by conformational changes in lysozyme due to interaction with carbon nanotubes. Complexes which are formed as a result of such interaction, have characteristic features of amyloid fibrillar structures. It reveals one of possible mechanisms of carbon nanotubes cytotoxicity. On the other hand, such a technique can be introduced to obtain model amyloid fibrils for further study.
Conclusion: The method of vibtarional spectroscopy has shown that carbon nanotubes can influence the structure of lysozyme, as it is shown by the conformational analysis of the absorption band Amide I. After the interaction of lysozyme with CNT, an increase in the contribution of antiparallel β-conformation in the structure of lysozyme is observed, and the contribution of the α-helix conformation is reduced, which are characteristic features in the formation of fibrillar structures. The possibility of amyloid fibril formation without the use of high temperatures at different pH values with the interaction of lysozyme and carbon nanotubes, which can be applied as a method for obtaining the model amyloid fibrils, is shown.
Downloads
References
Annamalai, K., Gührs, K.-H., Koehler, R., Schmidt, M., Michel, H., Loos, C., Fändrich, M. (2016). Polymorphism of Amyloid Fibrils In Vivo. AngewandteChemie International Edition, 55(15), 4822-4825.
Li, H., Luo, Y., Derreumaux, P., & Wei, G. (2011). Carbon Nanotube Inhibits the Formation of β-Sheet-Rich Oligomers of the Alzheimer’s Amyloid-β(16-22) Peptide. Biophysical Journal, 101(9), 2267–2276. https://doi.org/10.1016/j.bpj.2011.09.046
Close, W., Neumann, M., Schmidt, A., Hora, M., Annamalai, K., Schmidt, M., …Fändrich, M. (2018). Physical basis of amyloid fibril polymorphism. Nature Communications, 9(1). https://doi.org/10.1038/s41467-018-03164-5
Schmidt, A., Annamalai, K., Schmidt, M., Grigorieff, N., &Fändrich, M. (2016). Cryo-EM reveals the steric zipper structure of a light chain-derived amyloid fibril. Proceedings of the National Academy of Sciences, 113(22), 6200–6205. https://doi.org/10.1073/pnas.1522282113
Liberta, F., Loerch, S., Rennegarbe, M., Schierhorn, A., Westermark, P., Westermark, G. T., …Schmidt, M. (2018). Cryo-EM structure of an amyloid fibril from systemic amyloidosis. Cold Spring Harbor Laboratory. https://doi.org/10.1101/357129
Knubovets, T., Osterhout, J. J., Connolly, P. J., &Klibanov, A. M. (1999). Structure, thermostability, and conformational flexibility of hen egg-white lysozyme dissolved in glycerol. Proceedings of the National Academy of Sciences, 96(4), 1262–1267. https://doi.org/10.1073/pnas.96.4.1262
Zou, Y., Hao, W., Li, H., Gao, Y., Sun, Y., & Ma, G. (2014). New Insight into Amyloid Fibril Formation of Hen Egg White Lysozyme Using a Two-Step Temperature-Dependent FTIR Approach. The Journal of Physical Chemistry B, 118(33), 9834–9843. https://doi.org/10.1021/jp504201k
Riek, R., & Eisenberg, D. S. (2016). The activities of amyloids from a structural perspective. Nature, 539(7628), 227–235. https://doi.org/10.1038/nature20416
Sipe, J. D., Benson, M. D., Buxbaum, J. N., Ikeda, S., Merlini, G., Saraiva, M. J. M., &Westermark, P. (2016). Amyloid fibril proteins and amyloidosis: chemical identification and clinical classification International Society of Amyloidosis 2016 Nomenclature Guidelines. Amyloid, 23(4), 209–213. https://doi.org/10.1080/13506129.2016.1257986
Annamalai, K., Liberta, F., Vielberg, M.-T., Close, W., Lilie, H., Gührs, K.-H., …Fändrich, M. (2017). Common Fibril Structures Imply Systemically Conserved Protein Misfolding Pathways In Vivo. Angewandte Chemie International Edition, 56(26), 7510–7514. https://doi.org/10.1002/anie.201701761
Yuan, S., Deng, Q., Fang, G., Wu, J., Li, W., & Wang, S. (2014). Protein imprinted ionic liquid polymer on the surface of multiwall carbon nanotubes with high binding capacity for lysozyme. Journal of Chromatography B, 960, 239–246. https://doi.org/10.1016/j.jchromb.2014.04.021
Gao, R., Zhang, L., Hao, Y., Cui, X., Liu, D., Zhang, M., & Tang, Y. (2015). Novel polydopamine imprinting layers coated magnetic carbon nanotubes for specific separation of lysozyme from egg white. Talanta, 144, 1125–1132. https://doi.org/10.1016/j.talanta.2015.07.090
Horn, D. W., Tracy, K., Easley, C. J., & Davis, V. A. (2012). Lysozyme Dispersed Single-Walled Carbon Nanotubes: Interaction and Activity. The Journal of Physical Chemistry C, 116(18), 10341–10348. https://doi.org/10.1021/jp300242a
Vaitheeswaran, S., & Garcia, A. E. (2011). Protein stability at a carbon nanotube interface. The Journal of Chemical Physics, 134(12), 125101.https://doi.org/10.1063/1.3558776
Dovbeshko, G. I., Chegel, V. I., Gridina, N. Y., Repnytska, O. P., Shirshov, Y. M., Tryndiak, V. P., … Solyanik, G. I. (2002). Surface enhanced IR absorption of nucleic acids from tumor cells: FTIR reflectance study. Biopolymers, 67(6), 470–486. https://doi.org/10.1002/bip.10165
Dovbeshko, G.I. (2009). Molecular mechanisms of interaction of biological molecules with nanostructures, ligands and low doses of ionizing and microwave irradiation. (Doctor of sciences dissertation, V.N. Karazin Kharkiv National University, Kharkiv). (in Ukrainian). Available from Vernadsky National Library of Ukraine (DS117134)
Dovbeshko, G.I., Chegel, V.I., Gridina, N.Ya.,Gnatyuk, O.P., Shirshov, Y.M., Tryndiak, V.P., and Todor, I.M. (2001). Surface enhanced infrared absorption of nucleic acids on gold substrate. Semiconductor Physics Quantum Electronics and Optoelectronics, 4(3), 202-206. https://doi.org/10.1117/12.429717
Dong A., Meyer J.D., Brown J.L., Manning M.C., Carpenter J. F. (2000) Comparative Fourier Transform Infrared and Circular Dichroism spectroscopic analysis of a1l-proteinase inhibitor and ovalbumin in aqueous solution. Arch. Biochem. Biophys. 383: 148-155. https://doi.org/10.1006/abbi.2000.2054
Goormaghtigh, E., Ruysschaert, J.-M., &Raussens, V. (2006). Evaluation of the Information Content in Infrared Spectra for Protein Secondary Structure Determination. Biophysical Journal, 90(8), 2946–2957. https://doi.org/10.1529/biophysj.105.072017
Pérez, C., &Griebenow, K. (2000). Fourier-transform infrared spectroscopic investigation of the thermal denaturation of hen egg-white lysozyme dissolved in aqueous buffer and glycerol. Biotechnology Letters. 22(23), 1899–1905. https://doi.org/10.1023/a:1005645810247
Zandomeneghi, G., Krebs, M. R. H., McCammon, M. G., &Fändrich, M. (2009). FTIR reveals structural differences between native β-sheet proteins and amyloid fibrils. Protein Science, 13(12), 3314–3321. https://doi.org/10.1110/ps.041024904
del Mercato, L. L., Pompa, P. P., Maruccio, G., Torre, A. D., Sabella, S., Tamburro, A. M., …Rinaldi, R. (2007). Charge transport and intrinsic fluorescence in amyloid-like fibrils. Proceedings of the National Academy of Sciences, 104(46), 18019–18024. https://doi.org/10.1073/pnas.0702843104
Waters, J. C. (2009). Accuracy and precision in quantitative fluorescence microscopy. The Journal of Cell Biology, 185(7), 1135–1148. https://doi.org/10.1083/jcb.200903097
Churchman, L. S., Okten, Z., Rock, R. S., Dawson, J. F., & Spudich, J. A. (2005). Single molecule high-resolution colocalization of Cy3 and Cy5 attached to macromolecules measures intramolecular distances through time. Proceedings of the National Academy of Sciences, 102(5), 1419–1423. https://doi.org/10.1073/pnas.0409487102
Yildiz, A., &Selvin, P. R. (2005). Fluorescence Imaging with One Nanometer Accuracy: Application to Molecular Motors. Accounts of Chemical Research, 38(7), 574–582. https://doi.org/10.1021/ar040136s
Huang, B., W. Wang, M. Bates, and X. Zhuang. (2008). Three-dimensional super-resolution imaging by stochastic optical reconstruction microscopy. Science, 319, 810–813.
Manley, S., Gillette, J. M., Patterson, G. H., Shroff, H., Hess, H. F., Betzig, E., & Lippincott-Schwartz, J. (2008). High-density mapping of single-molecule trajectories with photoactivated localization microscopy. Nature Methods, 5(2), 155–157. https://doi.org/10.1038/nmeth.1176
Pawley J. B. (2006) Handbook of Biological Confocal Microscopy (3d ed.). Springer, New York: Science+Business Media, LLC.
Kovalska, V., Chernii, S., Cherepanov, V., Losytskyy, M., Chernii, V., Varzatskii, O., …Yarmoluk, S. (2017). The impact of binding of macrocyclic metal complexes on amyloid fibrillization of insulin and lysozyme. Journal of Molecular Recognition, 30(8), e2622. https://doi.org/10.1002/jmr.2622
Authors who publish with this journal agree to the following terms:
- Authors retain copyright and grant the journal right of first publication with the work simultaneously licensed under a Creative Commons Attribution License that allows others to share the work with an acknowledgement of the work's authorship and initial publication in this journal.
- Authors are able to enter into separate, additional contractual arrangements for the non-exclusive distribution of the journal's published version of the work (e.g., post it to an institutional repository or publish it in a book), with an acknowledgement of its initial publication in this journal.
- Authors are permitted and encouraged to post their work online (e.g., in institutional repositories or on their website) prior to and during the submission process, as it can lead to productive exchanges, as well as earlier and greater citation of published work (See The Effect of Open Access).
