|
|
|
|
| LEADER |
01000naa a22002652 4500 |
| 001 |
NLM345909631 |
| 003 |
DE-627 |
| 005 |
20231226030149.0 |
| 007 |
cr uuu---uuuuu |
| 008 |
231226s2022 xx |||||o 00| ||eng c |
| 024 |
7 |
|
|a 10.1107/S1600577522007330
|2 doi
|
| 028 |
5 |
2 |
|a pubmed24n1152.xml
|
| 035 |
|
|
|a (DE-627)NLM345909631
|
| 035 |
|
|
|a (NLM)36073871
|
| 040 |
|
|
|a DE-627
|b ger
|c DE-627
|e rakwb
|
| 041 |
|
|
|a eng
|
| 100 |
1 |
|
|a Jindo, Mikiko
|e verfasserin
|4 aut
|
| 245 |
1 |
0 |
|a Application study of infrared free-electron lasers towards the development of amyloidosis therapy
|
| 264 |
|
1 |
|c 2022
|
| 336 |
|
|
|a Text
|b txt
|2 rdacontent
|
| 337 |
|
|
|a ƒaComputermedien
|b c
|2 rdamedia
|
| 338 |
|
|
|a ƒa Online-Ressource
|b cr
|2 rdacarrier
|
| 500 |
|
|
|a Date Completed 09.09.2022
|
| 500 |
|
|
|a Date Revised 04.10.2022
|
| 500 |
|
|
|a published: Print-Electronic
|
| 500 |
|
|
|a Citation Status MEDLINE
|
| 520 |
|
|
|a open access.
|
| 520 |
|
|
|a Amyloidosis is known to be caused by the deposition of amyloid fibrils into various biological tissues; effective treatments for the disease are little established today. An infrared free-electron laser (IR-FEL) is an accelerator-based picosecond-pulse laser having tunable infrared wavelengths. In the current study, the irradiation effect of an IR-FEL was tested on an 11-residue peptide (NFLNCYVSGFH) fibril from β2-microglobulin (β2M) with the aim of applying IR-FELs to amyloidosis therapy. Infrared microspectroscopy (IRM) and scanning electron microscopy showed that a fibril of β2M peptide was clearly dissociated by IR-FEL at 6.1 µm (amide I) accompanied by a decrease of the β-sheet and an increase of the α-helix. No dissociative process was recognized at 6.5 µm (amide II) as well as at 5.0 µm (non-specific wavelength). Equilibrium molecular dynamics simulations indicated that the α-helix can exist stably and the probability of forming interchain hydrogen bonds associated with the internal asparagine residue (N4) is notably reduced compared with other amino acids after the β-sheet is dissociated by amide I specific irradiation. This result implies that N4 plays a key role for recombination of hydrogen bonds in the dissociation of the β2M fibril. In addition, the β-sheet was disrupted at temperatures higher than 340 K while the α-helix did not appear even though the fibril was heated up to 363 K as revealed by IRM. The current study gives solid evidence for the laser-mediated conversion from β-sheet to α-helix in amyloid fibrils at the molecular level
|
| 650 |
|
4 |
|a Journal Article
|
| 650 |
|
4 |
|a amyloid fibril
|
| 650 |
|
4 |
|a amyloidosis
|
| 650 |
|
4 |
|a infrared free-electron laser
|
| 650 |
|
4 |
|a β2-microglobulin
|
| 650 |
|
7 |
|a Amides
|2 NLM
|
| 650 |
|
7 |
|a Amyloid
|2 NLM
|
| 650 |
|
7 |
|a Peptides
|2 NLM
|
| 700 |
1 |
|
|a Nakamura, Kazuhiro
|e verfasserin
|4 aut
|
| 700 |
1 |
|
|a Okumura, Hisashi
|e verfasserin
|4 aut
|
| 700 |
1 |
|
|a Tsukiyama, Koichi
|e verfasserin
|4 aut
|
| 700 |
1 |
|
|a Kawasaki, Takayasu
|e verfasserin
|4 aut
|
| 773 |
0 |
8 |
|i Enthalten in
|t Journal of synchrotron radiation
|d 1994
|g 29(2022), Pt 5 vom: 01. Sept., Seite 1133-1140
|w (DE-627)NLM09824129X
|x 1600-5775
|7 nnns
|
| 773 |
1 |
8 |
|g volume:29
|g year:2022
|g number:Pt 5
|g day:01
|g month:09
|g pages:1133-1140
|
| 856 |
4 |
0 |
|u http://dx.doi.org/10.1107/S1600577522007330
|3 Volltext
|
| 912 |
|
|
|a GBV_USEFLAG_A
|
| 912 |
|
|
|a SYSFLAG_A
|
| 912 |
|
|
|a GBV_NLM
|
| 912 |
|
|
|a GBV_ILN_40
|
| 912 |
|
|
|a GBV_ILN_350
|
| 912 |
|
|
|a GBV_ILN_2005
|
| 951 |
|
|
|a AR
|
| 952 |
|
|
|d 29
|j 2022
|e Pt 5
|b 01
|c 09
|h 1133-1140
|