{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,24]],"date-time":"2026-08-24T21:16:51Z","timestamp":1787606211143,"version":"build-2736575974"},"reference-count":99,"publisher":"MDPI AG","issue":"4","license":[{"start":{"date-parts":[[2023,2,12]],"date-time":"2023-02-12T00:00:00Z","timestamp":1676160000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001691","name":"Japan Society for the Promotion of Science KAKENHI","doi-asserted-by":"publisher","award":["JP20K12483"],"award-info":[{"award-number":["JP20K12483"]}],"id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Amyloid fibril causes serious amyloidosis such as neurodegenerative diseases. The structure is composed of rigid \u03b2-sheet stacking conformation which makes it hard to disassemble the fibril state without denaturants. Infrared free electron laser (IR-FEL) is an intense picosecond pulsed laser that is oscillated through a linear accelerator, and the oscillation wavelengths are tunable from 3 \u03bcm to 100 \u03bcm. Many biological and organic compounds can be structurally altered by the mode-selective vibrational excitations due to the wavelength variability and the high-power oscillation energy (10\u201350 mJ\/cm2). We have found that several different kinds of amyloid fibrils in amino acid sequences were commonly disassembled by the irradiation tuned to amide I (6.1\u20136.2 \u03bcm) where the abundance of \u03b2-sheet decreased while that of \u03b1-helix increased by the vibrational excitation of amide bonds. In this review, we would like to introduce the IR-FEL oscillation system briefly and describe combination studies of experiments and molecular dynamics simulations on disassembling amyloid fibrils of a short peptide (GNNQQNY) from yeast prion and 11-residue peptide (NFLNCYVSGFH) from \u03b22-microglobulin as representative models. Finally, possible applications of IR-FEL for amyloid research can be proposed as a future outlook.<\/jats:p>","DOI":"10.3390\/ijms24043686","type":"journal-article","created":{"date-parts":[[2023,2,13]],"date-time":"2023-02-13T03:28:46Z","timestamp":1676258926000},"page":"3686","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":5,"title":["Disassembly of Amyloid Fibril with Infrared Free Electron Laser"],"prefix":"10.3390","volume":"24","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-8376-5807","authenticated-orcid":false,"given":"Takayasu","family":"Kawasaki","sequence":"first","affiliation":[{"name":"Accelerator Laboratory, High Energy Accelerator Research Organization, 1-1 Oho, Tsukuba 305-0801, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Koichi","family":"Tsukiyama","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Faculty of Science Division I, Tokyo University of Science, 1-3 Kagurazaka, Tokyo 184-8501, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Phuong H.","family":"Nguyen","sequence":"additional","affiliation":[{"name":"CNRS, UPR 9080, Laboratoire de Biochimie Th\u00e9orique, Institut de Biologie Physico-Chimique, Fondation Edmond de Rothschild, Universit\u00e9 Paris Cit\u00e9, 13 Rue Pierre et Marie Curie, 75005 Paris, France"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2023,2,12]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"777","DOI":"10.1007\/s00401-013-1125-6","article-title":"Protein aggregation in amyotrophic lateral sclerosis","volume":"125","author":"Blokhuis","year":"2013","journal-title":"Acta Neuropathol."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"1479","DOI":"10.1080\/19420862.2019.1658493","article-title":"Protein aggregation and mitigation strategy in low pH viral inactivation for monoclonal antibody purification","volume":"11","author":"Jin","year":"2019","journal-title":"mAbs"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"107573","DOI":"10.1016\/j.biotechadv.2020.107573","article-title":"Protein folding and assembly in confined environments: Implications for protein aggregation in hydrogels and tissues","volume":"42","author":"Simpson","year":"2020","journal-title":"Biotechnol. 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