Skip to main content
SpringerLink
Log in

Study on Irradiation Effect of Mid-Infrared Free Electron Laser on Hen Egg-White Lysozyme by Using Terahertz-Time Domain Spectroscopy and Synchrotron-Radiation Vacuum-Ultraviolet Circular-Dichroism Spectroscopy

  • Published:
Journal of Infrared, Millimeter, and Terahertz Waves Aims and scope Submit manuscript

Abstract

Mid-infrared free-electron laser (MIR-FEL) is potentially applicable for tissue ablation and dissociation of pathological peptide aggregates in medicine. However, it is still poorly understood how the MIR-FEL irradiation influences on functional proteins such as enzymes. In the current study, the effect of MIR-FEL on both aggregate and non-aggregate (= native) states of hen egg-white lysozyme (HEWL) as a representative enzyme has been investigated. Absorption intensity at terahertz region (0.3–1.2 THz, 10–40 cm−1) of the aggregate of HEWL was lower than that of the native HEWL, but the former was increased nearly to the same level with the latter after the MIR-FEL irradiation tuned to 6 μm that corresponds to carbonyl stretching vibrational mode of amide bonds (amide I). This indicates that the aggregate of HEWL was converted to the native state by the irradiation. On the other hand, synchrotron-radiation vacuum-ultraviolet circular-dichroism spectroscopy showed that protein conformation of the native HEWL, which was rich in α-helix, was little changed after the MIR-FEL irradiation under the same condition with the case of the aggregate of HEWL. Furthermore, the enzymatic hydrolysis activity of the native HEWL against bacterial glycan was not remarkably decreased by the irradiation. Therefore, it can be estimated that the native structure of HEWL is little damaged although the aggregate state can be easily dissociated by the resonant excitation at amide bonds.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Fig. 1
Fig. 2
Fig. 3
Fig. 4

Similar content being viewed by others

References

  1. P.G. O’Shea and H.P. Freund, Free-Electron Lasers: Status and Applications, Science 292 (2001), no.5523, 1853–1858.

    Article  Google Scholar 

  2. F. Glotin, R. Chaput, D. Jaroszynski, R. Prazeres, and J. Ortega, Infrared subpicosecond laser pulses with a free-electron laser, Phys Rev Lett. 71 (1993), no.16, 2587–2590.

    Article  Google Scholar 

  3. K. Cohn, J. Blau, W.B. Colson, J. Ng, and M. Price, Free electron Lasers in 2015, Proceedings of FEL 2015 (2015), 625–629.

    Google Scholar 

  4. G. Edwards, R. Logan, M. Copeland, L. Reinisch, J. Davidson, B. Johnson, R. Maciunas, M. Mendenhall, R. Ossoff, J. Tribble, J. Werkhaven, and D. O’Day, Tissue ablation by a free-electron laser tuned to the amide II band, Nature 371 (1994), no.6496, 416–419.

    Article  Google Scholar 

  5. M.A. Mackanos, J.A. Kozub, and E.D. Jansen, The effect of free-electron laser pulse structure on mid-infrared soft-tissue ablation: ablation metrics, Phys. Med. Biol. 50 (2005), no.8, 1871–1883.

    Article  Google Scholar 

  6. G. Frison, G. van der Rest, F. Tureček, T. Besson, J. Lemaire, P. Maître, and J. Chamot-Rooke, Structure of electron-capture dissociation fragments from charge-tagged peptides probed by tunable infrared multiple photon dissociation, J. Am. Chem. Soc. 130 (2008), no.45, 14916–14917.

    Article  Google Scholar 

  7. R.H. Austin, A. Xie, L. van der Meer, B. Redlich, P. Lindgård, H. Frauenfelder, and D. Fu, Picosecond thermometer in the amide I band of myoglobin. Phys. Rev. Lett. 94 (2005),no.12, 128101.

  8. L. Jašíková and J. Roithová, Infrared Multiphoton Dissociation Spectroscopy with Free-Electron Lasers: On the Road from Small Molecules to Biomolecules, Chemistry 24 (2018), no.14, 3374–3390.

    Article  Google Scholar 

  9. M. Matsubara, F. Osada, M. Nakajima, T. Imai, K. Nishimura, T. Oyama, and K. Tsukiyama, Isomerization and dissociation of 2,3-dihydrofuran (2,3-DHF) induced by infrared free electron laser, J. Photochem. Photobiol. A 322 (2016), 53–59.

    Article  Google Scholar 

  10. Y. Xiao, M. Guo, P. Zhang, G. Shanmugam, P.L. Polavarapu, and M.S. Hutson, Wavelength-dependent conformational changes in collagen after mid-infrared laser ablation of cornea, Biophys. J. 94 (2008), no.4, 1359–1366.

    Article  Google Scholar 

  11. T. Kawasaki, T. Yaji, T. Ohta, and K. Tsukiyama, Application of mid-infrared free-electron laser tuned to amide bands for dissociation of aggregate structure of protein, J. Synchrotron Rad. 23 (2016), no.1, 152–157.

    Article  Google Scholar 

  12. T. Kawasaki, T. Yaji, T. Ohta, K. Tsukiyama, and K. Nakamura, Dissociation of β-sheet stacking of amyloid β fibrils by irradiation of intense, short-pulsed mid-infrared laser, Cell. Mol. Neurobiol. 38 (2018), .no.5, 1039–1049.

    Article  Google Scholar 

  13. D.J. Vocadlo, G.J. Davies, R. Laine, and S.G. Withers, Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate, Nature 412 (2001), .no.6849, 835–838.

    Article  Google Scholar 

  14. M.R.H. Krebs, D.K. Wilkins, E.W. Chung, M.C. Pitkeathly, A.K. Chamberlain, J. Zurdo, C.V. Robinson, and C.M. Dobson, Formation and seeding of amyloid fibrils from wild-type hen lysozyme and a peptide fragment from the β-domain, J. Mol. Biol. 300 (2000), no.3, 541–549.

    Article  Google Scholar 

  15. J. Knab, J-Y. Chen, and A. Markelz, Hydration dependence of conformational dielectric relaxation of lysozyme. Biophys. J. 90 (2006), no.7, 2576–2581.

    Article  Google Scholar 

  16. K. Matsuo and K. Gekko, Construction of a synchrotron-radiation vacuum-ultraviolet circular-dichroism spectrophotometer and its application to the structural analysis of biomolecules, Bull. Chem. Soc. Jpn. 86 (2013), no.6, 675–689.

  17. M. Hangyo, M. Tani, and T. Nagashima, Terahertz time-domain spectroscopy of solids: a review, Int. J. Infrared Milli. Waves 26 (2005), no.12, 1661–1690.

    Article  Google Scholar 

  18. K. Gekko and K. Matsuo, Vacuum-ultraviolet circular dichroism analysis of biomolecules, Chirality 18 (2006), no.5, 329–334.

    Article  Google Scholar 

  19. K. Matsuo, Y. Maki, H. Namatame, M. Taniguchi, and K. Gekko, Conformation of membrane-bound proteins revealed by vacuum-ultraviolet circular-dichroism and linear-dichroism spectroscopy, Proteins 84 (2016), no.3, 349–359.

    Article  Google Scholar 

  20. K. Matsuo, K. Sakai, Y. Matsushima, T. Fukuyama, and K. Gekko, Optical cell with a temperature-control unit for a vacuum-ultraviolet circular dichroism spectrophotometer, Anal. Sci. 19 (2003), no.1, 129–132.

    Article  Google Scholar 

  21. D. Thirumalai, G. Reddy, and J.E. Straub, Role of water in protein aggregation and amyloid polymorphism, Acc. Chem. Res. 45 (2012), no.1, 83–92.

    Article  Google Scholar 

  22. J. Xu, K.W. Plaxco, and S.J. Allen, Probing the collective vibrational dynamics of a protein in liquid water by terahertz absorption spectroscopy, Protein Sci. 15 (2006), no.5, 1175–1181.

    Article  Google Scholar 

  23. H. Naiki, K. Higuchi, M. Hosokawa, and T. Takeda, Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavin T1, Anal. Biochem. 177 (1989), no.2, 244–249.

    Article  Google Scholar 

  24. D. Morshedi, N. Rezaei-Ghaleh, A. Ebrahim-Habibi, S. Ahmadian, and M. Nemat-Gorgani, Inhibition of amyloid fibrillation of lysozyme by indole derivatives—possible mechanism of action, FEBS J. 274 (2007), no.24, 6415–6425.

    Article  Google Scholar 

  25. Y. Tokunaga, Y. Sakakibara, Y. Kamada, K. Watanabe, and Y. Sugimoto, Analysis of core region from egg white lysozyme forming amyloid fibrils, Int. J. Biol. Sci. 9 (2013), no.2, 219–227.

    Article  Google Scholar 

  26. P. Cecchini, G. Franceschi, E. Frare, A. Fontana, and P. Polverino de Laureto, The role of tryptophan in protein fibrillogenesis: relevance of Trp7 and Trp14 to the amyloidogenic properties of myoglobin, Protein Eng. Des. Sel. 25 (2012), no.4, 199–203.

  27. M.H. Viet, P. Derreumaux, M.S. Li, C. Roland, C. Sagui, and P.H. Nguyen, Picosecond dissociation of amyloid fibrils with infrared laser: a nonequilibrium simulation study, J. Chem. Phys. 143 (2015), no.15, 155101.

  28. M.S. Hutson, S.A. Hauger, and G. Edwards, Thermal diffusion and chemical kinetics in laminar biomaterial due to heating by a free-electron laser, Phys. Rev E. 65 (2002), no.6, 061906.

  29. A.J. Baldwin, T.P. Knowles, G.G. Tartaglia, A.W. Fitzpatrick, G.L. Devlin, S.L. Shammas, C.A. Waudby, M.F. Mossuto, S. Meehan, S.L. Gras, J. Christodoulou, S.J. Anthony-Cahill, P.D. Barker, M. Vendruscolo, and C.M. Dobson, Metastability of native proteins and the phenomenon of amyloid formation, J. Am. Chem. Soc. 133 (2011), no.36, 14160–14163.

    Article  Google Scholar 

  30. W. Wagner, A. Sokolow, R. Pearlstein, and G. Edwards, Thermal Vapor Bubble and Pressure Dynamics during Infrared Laser Ablation of Tissue, Appl. Phys. Lett. 94 (2009), no.1, 013901–1-3.

    Article  Google Scholar 

  31. R. R. Anderson and J. A. Parrish, Selective photothermolysis: precise microsurgery by selective absorption of pulsed radiation, Science 220 (1983), no.4596, 524–527.

    Article  Google Scholar 

  32. C. Pleyer, J. Flesche, and F. Saeed, Lysozyme amyloidosis – a case report and review of the literature, Clin. Nephrol. Case Stud. 3 (2015), 42–45.

    Google Scholar 

  33. M.B. Pepys, P.N. Hawkins, D.R. Booth, D.M. Vigushin, G.A. Tennent, A.K. Soutar, N. Totty, O. Nguyen, C.C.F. Blake, C.J. Terry, T.G. Feest, A.M. Zalin, and J.J. Hsuan, Human lysozyme gene mutations cause hereditary systemic amyloidosis, Nature 362 (1993), no.6420, 553–557.

    Article  Google Scholar 

Download references

Acknowledgments

We are grateful to the staff of the IR-FEL Research Center at Tokyo University of Science for providing the beam time. This work was supported in part by the Open Advanced Research Facilities Initiative and Photon Beam Platform Project of the Ministry of Education, Culture, Sports, Science and Technology of Japan, and the collaborative research project of the Research Center for Development of the Far-Infrared Region, University of Fukui, in the fiscal year 2016 (subject number: H28FIRDM029A). VUV-CD spectroscopy was carried out with the approval of the Hiroshima Synchrotron Radiation Center of Hiroshima University (proposal number: 17AU009).

Author information

Authors and Affiliations

  1. IR-FEL Research Center, Research Institute for Science and Technology, Organization for Research Advancement, Tokyo University of Science, 2641 Yamazaki, Noda, Chiba, 278-8510, Japan

    Takayasu Kawasaki, Gaku Ohori & Koichi Tsukiyama

  2. Hiroshima Synchrotron Radiation Center, Hiroshima University, 2-313 Kagamiyama, Higashi-Hiroshima, Hiroshima, 739-0046, Japan

    Yudai Izumi & Koichi Matsuo

  3. Research Center for Development of Far-Infrared Region, University of Fukui, 3-9-1 Bunkyo, Fukui, Fukui, 910-8507, Japan

    Hideaki Kitahara, Takashi Furuya, Kohji Yamamoto & Masahiko Tani

Authors
  1. Takayasu Kawasaki
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Yudai Izumi
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Gaku Ohori
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Hideaki Kitahara
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. Takashi Furuya
    View author publications

    You can also search for this author in PubMed Google Scholar

  6. Kohji Yamamoto
    View author publications

    You can also search for this author in PubMed Google Scholar

  7. Koichi Matsuo
    View author publications

    You can also search for this author in PubMed Google Scholar

  8. Masahiko Tani
    View author publications

    You can also search for this author in PubMed Google Scholar

  9. Koichi Tsukiyama
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Takayasu Kawasaki.

Ethics declarations

Conflict of Interest

The authors declare that they have no conflict of interest.

Additional information

Publisher’s Note

Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.

Electronic supplementary material

Rights and permissions

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Kawasaki, T., Izumi, Y., Ohori, G. et al. Study on Irradiation Effect of Mid-Infrared Free Electron Laser on Hen Egg-White Lysozyme by Using Terahertz-Time Domain Spectroscopy and Synchrotron-Radiation Vacuum-Ultraviolet Circular-Dichroism Spectroscopy. J Infrared Milli Terahz Waves 40, 998–1009 (2019). https://doi.org/10.1007/s10762-019-00626-9

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s10762-019-00626-9

Keywords

Search

Navigation