A partially folded structure of amyloid-beta(1-40) in an aqueous environment

被引：360
作者：
Vivekanandan, Subramanian [1 ,2 ]
Brender, Jeffrey R. [1 ,2 ]
Lee, Shirley Y. [2 ]
Ramamoorthy, Ayyalusamy [1 ,2 ]
机构：
[1] Univ Michigan, Dept Chem, Ann Arbor, MI 48109 USA
[2] Univ Michigan, Dept Biophys, Ann Arbor, MI 48109 USA
来源：
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2011年 / 411卷 / 02期
关键词：
Structure; Amyloid-beta; Alzheimer's; Disordered protein; Mis folding; Amyloidogenesis; AMYLOID-BETA-PEPTIDES; ALZHEIMERS-DISEASE; NMR-SPECTROSCOPY; RANDOM COIL; STATE; DYNAMICS; MONOMER; AMYLOIDOGENESIS; IDENTIFICATION; CONFORMATIONS;
D O I：
10.1016/j.bbrc.2011.06.133
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Aggregation of the A beta(1-40) peptide is linked to the development of extracellular plaques characteristic of Alzheimer's disease. While previous studies commonly show the A beta(1-40) is largely unstructured in solution, we show that A beta(1-40) can adopt a compact, partially folded structure. In this structure (PDB ID: 2LFM), the central hydrophobic region of the peptide forms a 3(10) helix from H13 to D23 and the Nand C-termini collapse against the helix due to the clustering of hydrophobic residues. Helical intermediates have been predicted to be crucial on-pathway intermediates in amyloid fibrillogenesis, and the structure presented here presents a new target for investigation of early events in A beta(1-40) fibrillogenesis. (C) 2011 Elsevier Inc. All rights reserved.
引用
收藏
页码：312 / 316
页数：5
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