Optical beam transport system at FEL-SUT

Nomaru, Keiji; Kawai, Masayuki; Yokoyama, Minoru; Oda, Fumihiko; Nakayama, Akihiro; Koike, Harutaka; Kuroda, Haruo

doi:10.1016/s0168-9002(00)00087-5

Cited by 16 publications

(7 citation statements)

References 1 publication

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“…1 . The structure and the features of FEL-TUS have been described in previous studies [ 16 , 27 ]. In brief, FEL is an apparatus that generates a laser beam using synchrotron radiation as a seed, with a variable wavelength within the mid-infrared region of 5–16 μm (625–2,000 cm −1 ).…”

Section: Methodsmentioning

confidence: 99%

Effect of Mid-infrared Free-Electron Laser Irradiation on Refolding of Amyloid-Like Fibrils of Lysozyme into Native Form

et al. 2012

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Aggregation of lysozyme in an acidic solution generates inactive amyloid-like fibrils, with a broad infrared peak appearing at 1,610–1,630 cm−1, characteristic of a β-sheet rich structure. We report here that spontaneous refolding of these fibrils in water could be promoted by mid-infrared free-electron laser (mid-IR FEL) irradiation targeting the amide bands. The Fourier transform infrared spectrum of the fibrils reflected a β-sheet content that was as low as that of the native structure, following FEL irradiation at 1,620 cm−1 (amide I band); both transmission-electron microscopy imaging and Congo Red assay results also demonstrated a reduced fibril structure, and the enzymatic activity of lysozyme fibrils recovered to 70–90 % of the native form. Both irradiations at 1,535 cm−1(amide II band) and 1,240 cm−1 (amide III band) were also more effective for the refolding of the fibrils than mere heating in the absence of FEL. On the contrary, either irradiation at 1,100 or 2,000 cm−1 afforded only about 60 % recovery of lysozyme activity. These results indicate that the specific FEL irradiation tuned to amide bands is efficient in refolding of lysozyme fibrils into native form.

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Section: Methodsmentioning

confidence: 99%

Effect of Mid-infrared Free-Electron Laser Irradiation on Refolding of Amyloid-Like Fibrils of Lysozyme into Native Form

et al. 2012

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“…In any case, one conclusion from these studies is that FEL irradiation can induce major changes in the higher-order structure of protein matrices. We are attempting to apply the IR free-electron laser at Tokyo University of Science (FEL-TUS) to biomedical techniques and to supply the FEL beam to biomedical users all over the world; as an application example, the amyloid aggregate was targeted [ 13 , 14 ]. Amyloid proteins reported thus far can be roughly divided into two categories (Tables 1 and 2 ): those that are related to neurodegenerative diseases (Table 1 ) and those that are not (Table 2 ).…”

Section: Introductionmentioning

confidence: 99%

Mid-infrared free-electron laser tuned to the amide I band for converting insoluble amyloid-like protein fibrils into the soluble monomeric form

et al. 2014

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A mid-infrared free-electron laser (FEL) is operated as a pulsed and linearly polarized laser with tunable wavelengths within infrared region. Although the FEL can ablate soft tissues with minimum collateral damage in surgery, the potential of FEL for dissecting protein aggregates is not fully understood. Protein aggregates such as amyloid fibrils are in some cases involved in serious diseases. In our previous study, we showed that amyloid-like lysozyme fibrils could be disaggregated into the native form with FEL irradiation specifically tuned to the amide I band (1,620 cm−1). Here, we show further evidence for the FEL-mediated disaggregation of amyloid-like fibrils using insulin fibrils. Insulin fibrils were prepared in acidic solution and irradiated by the FEL, which was tuned to either 1,620 or 2,000 cm−1 prior to the experiment. The Fourier transform infrared spectroscopy (FT-IR) spectrum after irradiation with the FEL at 1,620 cm−1 indicated that the broad peak (1,630–1,660 cm−1) became almost a single peak (1,652 cm−1), and the β-sheet content was reduced to 25 from 40 % in the fibrils, while that following the irradiation at 2,000 cm−1 remained at 38 %. The Congo Red assay as well as transmission electron microscopy observation confirmed that the number of fibrils was reduced by FEL irradiation at the amide I band. Size-exclusion chromatography analysis indicated that the disaggregated form of fibrils was the monomeric form. These results confirm that FEL irradiation at the amide I band can dissect amyloid-like protein fibrils into the monomeric form in vitro.

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“…Details regarding the principles of operation and characteristics of the FEL are described elsewhere. [18][19][20] The FEL system was coupled to a BioAPEX III FTICR mass spectrometer equipped with a 4.7 T superconducting magnet (Bruker Daltonics, Billerica, MA).…”

Section: Introductionmentioning

confidence: 99%

Infrared Multiphoton Dissociation Spectroscopic Analysis of Peptides and Oligosaccharides by Using Fourier Transform Ion Cyclotron Resonance Mass Spectrometry with a Midinfrared Free-Electron Laser

et al. 2006

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The fragmentation of peptides and oligosaccharides in the gas phase was investigated by means of electrospray ionization Fourier transform ion cyclotron resonance (FTICR) mass spectrometry coupled with dissociation by a laser-cleavage infrared multiphoton dissociation (IRMPD) technique. In this technique, an IR free-electron laser is used as a tunable source of IR radiation to cause cleavage of the ionized samples introduced into the FTICR cell. The gas-phase IRMPD spectra of protonated peptides (substance P and angiotensin II) and two sodiated oligosaccharides (sialyl Lewis X and lacto-N-fucopentaose III) were obtained over the IR scan range of 5.7-9.5 microm. In the IRMPD spectra for the peptide, fragment ions are observed as y/b-type fragment ions in the range 5.7-7.5 microm, corresponding to cleavage of the backbone of the parent amino acid sequence, whereas the spectra of the oligosaccharides have major peaks in the range 8.4-9.5 microm, corresponding to photoproducts of the B/Y type.

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Optical beam transport system at FEL-SUT

Cited by 16 publications

References 1 publication

Effect of Mid-infrared Free-Electron Laser Irradiation on Refolding of Amyloid-Like Fibrils of Lysozyme into Native Form

Effect of Mid-infrared Free-Electron Laser Irradiation on Refolding of Amyloid-Like Fibrils of Lysozyme into Native Form

Mid-infrared free-electron laser tuned to the amide I band for converting insoluble amyloid-like protein fibrils into the soluble monomeric form

Infrared Multiphoton Dissociation Spectroscopic Analysis of Peptides and Oligosaccharides by Using Fourier Transform Ion Cyclotron Resonance Mass Spectrometry with a Midinfrared Free-Electron Laser

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