Synchrotron-Radiation Infrared Microscopy Analysis of an Amyloid Peptide Irradiated by Mid-Infrared Free-Electron Laser | ||
| Iraqi Journal of Applied Physics | ||
| Article 1, Volume 14, Issue 3, December 2018, Pages 41-45 | ||
| Author | ||
| Maisun R. Elewi | ||
| Abstract | ||
| In this work, we have irradiated amyloid fibrils with a free-electron laser (FEL) tuned to mid-infrared frequencies to induce dissociation of the aggregates into monomer forms. Synchrotron-radiation infrared microscopy (SR-IRM) is a powerful tool for in situ analysis of minute structural changes of various materials, and in this study, the feasibility of SR-IRM for analyzing the microscopic conformational changes of amyloid fibrils of a peptide after FEL irradiation was investigated. Reflection spectra of the amyloid fibril surface showed that the amide I peaks shifted to higher wavenumbers after the FEL irradiation, indicating that the initial β-sheet-rich structure transformed into a mixture of non-ordered and turn-like peptide conformations. This result demonstrates that conformational changes of the fibril structure after the FEL irradiation can be observed at a high spatial resolution using SR-IRM analysis and the FEL irradiation system can be useful for dissociation of amyloid aggregates. | ||
| Keywords | ||
| Infrared Microscopy Analysis; Amyloid Peptide; free; Electron Laser; Synchrotron; Radiation | ||
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