原创力文档deciphering the structure, growth and assembly of amyloid-like fibrils using high-speed atomic force microscopy解密的结构、生长和组装amyloid-like纤维使用高速原子力显微镜.pdfVIP
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deciphering the structure, growth and assembly of amyloid-like fibrils using high-speed atomic force microscopy解密的结构、生长和组装amyloid-like纤维使用高速原子力显微镜
Deciphering the Structure, Growth and Assembly of
Amyloid-Like Fibrils Using High-Speed Atomic Force
Microscopy
1,2 . 3. 1,2 1,2
Pierre-Emmanuel Milhiet * , Daisuke Yamamoto , Olivia Berthoumieu , Patrice Dosset , Christian
1,2 4 ´ 4 3
Le Grimellec , Jean-Michel Verdier , Stephane Marchal , Toshio Ando
´
1 Inserm, U 554, Montpellier, France, 2 Universite de Montpellier, CNRS, UMR 5048, Centre de Biochimie Structurale, Montpellier, France, 3 Department of Physics,
´
Graduate School of Science and Technology, Kanazawa University, Kanazawa, Japan, 4 Inserm, U710, Montpellier, France; Universite de Montpellier 2, Montpellier, France;
EPHE, Paris, France
Abstract
Formation of fibrillar structures of proteins that deposit into aggregates has been suggested to play a key role in various
neurodegenerative diseases. However mechanisms and dynamics of fibrillization remains to be elucidated. We have
previously established that lithostathine, a protein overexpressed in the pre-clinical stages of Alzheimer’s disease and
present in the pathognomonic lesions associated with this disease, form fibrillar aggregates after its N-terminal truncation.
In this paper we visualized, using high-speed atomic force microscopy (HS-AFM), growth and assembly of lithostathine
protofibrils under physiological conditions with a time resolution of one ima
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