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题名: Spectroscopic Evidence for Polymorphic Aggregates Formed by Amyloid-beta Fragments
作者: Guo, Yangmei1;  Wang, Jianping1
关键词: amyloid beta-peptides ;  IR spectroscopy ;  aggregation ;  electron microscopy ;  protein structures
刊名: CHEMPHYSCHEM
发表日期: 2012-12-07
DOI: 10.1002/cphc.201200611
卷: 13, 期:17, 页:3901-3908
收录类别: SCI
文章类型: Article
WOS标题词: Science & Technology ;  Physical Sciences
类目[WOS]: Chemistry, Physical ;  Physics, Atomic, Molecular & Chemical
研究领域[WOS]: Chemistry ;  Physics
英文摘要: Understanding the structure of amyloid-beta (A beta) aggregates is a key step towards elucidating the pathology of Alzheimers disease. In this work, three fragments of the A beta 142 protein, A beta 125 (DAEFRHDSGYEVHHQKLVFFAEDVG), A beta 2535 (GSNKGAIIGLM), and A beta 3342 (GLMVGGVVIA), were synthesized, and their aggregated structures were examined by linear infrared spectroscopy in the amide-I (mainly the C?O stretching) region. The structures of the formed aggregates were found to be both sequence and pH dependent. The results suggest that instead of forming matured fibrils, as in the case of full-length A beta 142, both A beta 125 and A beta 3342 form a mixture of threadlike beta-sheet fibril, soluble beta-sheet oligomer, and random coil structures. The beta-sheet conformations were found to be mainly antiparallel for the former and both parallel and antiparallel for the latter. However, the A beta 2535 fragment was found to form assembled fibrils containing predominantly parallel beta-sheets. The conformation and morphology of the aggregates were also confirmed by circular dichroism measurements and transmission electron microscopy. Factors influencing the structures of the aggregates formed by the A beta fragments were discussed.
关键词[WOS]: 2-DIMENSIONAL INFRARED-SPECTROSCOPY ;  PROTEIN SECONDARY STRUCTURE ;  CHAIN PLEATED SHEET ;  AMIDE-ONE VIBRATION ;  SOLID-STATE NMR ;  FIBRIL FORMATION ;  CIRCULAR-DICHROISM ;  ALZHEIMERS-DISEASE ;  STRUCTURAL MODEL ;  EXPERIMENTAL CONSTRAINTS
语种: 英语
WOS记录号: WOS:000312038200022
Citation statistics: 
内容类型: 期刊论文
URI标识: http://cas-ir.dicp.ac.cn/handle/321008/143130
Appears in Collections:中国科学院大连化学物理研究所_期刊论文

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作者单位: 1.Chinese Acad Sci, Inst Chem, State Key Lab Mol React Dynam, Beijing Natl Lab Mol Sci, Beijing 100190, Peoples R China

Recommended Citation:
Guo, Yangmei,Wang, Jianping. Spectroscopic Evidence for Polymorphic Aggregates Formed by Amyloid-beta Fragments[J]. CHEMPHYSCHEM,2012,13(17):3901-3908.
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