Trace Copper(II) or Zinc(II) Ions Drastically Modify the Aggregation Behavior of Amyloid-β1-42: An AFM Study

被引:74
作者
Innocenti, Massimo [1 ]
Salvietti, Emanuele [1 ]
Guidotti, Martina [1 ]
Casini, Angela [3 ]
Bellandi, Silvano [1 ]
Foresti, Maria Luisa [1 ]
Gabbiani, Chiara [1 ]
Pozzi, Andrea [1 ]
Zatta, Paolo [2 ]
Messori, Luigi [1 ]
机构
[1] Univ Florence, Dept Chem, I-50019 Sesto Fiorentino, Italy
[2] Univ Padua, Dept Biol, CNR Inst Biomed Technol, Padova Met Prot Unit, Padua, Italy
[3] Ecole Polytech Fed Lausanne, Inst Sci & Ingn Chim, CH-1015 Lausanne, Switzerland
基金
瑞士国家科学基金会;
关键词
Alzheimer's disease; amyloid-beta; atomic force microscopy; metal ions; BETA-AMYLOID AGGREGATION; ALZHEIMERS-DISEASE; METAL-IONS; A-BETA; CHELATION-THERAPY; INSIGHTS; IRON; METALLOBIOLOGY; PROTOFIBRILS; ALUMINUM;
D O I
10.3233/JAD-2010-1338
中图分类号
Q189 [神经科学];
学科分类号
071006 ;
摘要
Formation of amyloid-beta (A beta)(1-42) amyloid fibrils, a characteristic feature of Alzheimer's disease (AD), was monitored in situ through atomic force microscopy (AFM). Well-structured amyloid fibrils slowly formed in solution within 24 hours for which high quality AFM pictures could be obtained. Remarkably, addition of either copper(II) or zinc(II) ions to the incubation medium, even at extremely low molar ratios, dramatically changed the A beta(1-42) aggregation profile and prevented fibril formation. Aggregates of different morphology appeared in accordance with previous observations: small globular aggregates upon addition of zinc; ill-structured micro-aggregates in the case of copper. The implications of these AFM results are discussed in the context of current concepts for AD metallobiology.
引用
收藏
页码:1323 / 1329
页数:7
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