Structural remodeling during amyloidogenesis of physiological Nα-acetylated α-synuclein
详细信息 查看全文
- 作者：J. Ignacio Galleaa ; Rabia Sarroukhb ; Pablo Yunes-Quartinoa ; Jean-Marie Ruysschaertb ; Vincent Raussensb ; M. Soledad Celeja ; mcelej@mail.fcq.unc.edu.ar" class="auth_mail" title="E-mail the corresponding author
- 关键词：AS ; α-synuclein ; Ac-AS ; acetylated α-synuclein ; mAS ; oAS ; fAS ; α-synuclein monomers ; oligomers and fibrils respectively ; mAc-AS ; oAc-AS ; fAc-AS ; acetylated α-synuclein monomers ; oligomers and fibrils respectively ; NatB ; N-terminal acetyltransferase B ; IPTG ; isopropyl-β-d-1-galactopyranoside ; ThioT ; Thioflavin T ; 1 ; 8-ANS ; 1-anilino-naphthalene-8-sulfonate ; POPG ; 1-palmitoyl ; 2-oleoyl phosphatidylglycerol ; LUVs ; large unilamellar vesicles ; FPLC ; fast protein liquid chromatography ; SEC ; size-exclus
- 刊名：Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
- 出版年：2016
- 出版时间：May 2016
- 年：2016
- 卷：1864
- 期：5
- 页码：501-510
- 全文大小：1501 K
文摘
- •
Conformational ensembles of acetylated α-synuclein are alike the unmodified protein.
- •
Aggregation of acetylated α-synuclein involves antiparallel β-sheet intermediates.
- •
Fibril formation demands β-sheet remodeling mediated by helical/disordered species.
- •
The regions involved in structural rearrangements during aggregation are proposed.