Self-Propagating, Molecular-Level Polymorphism in Alzheimer's beta-Amyloid Fibrils Export

@article{citeulike:2537735, abstract = {Amyloid fibrils commonly exhibit multiple distinct morphologies in electron microscope and atomic force microscope images, often within a single image field. By using electron microscopy and solid-state nuclear magnetic resonance measurements on fibrils formed by the 40-residue {beta}-amyloid peptide of Alzheimer's disease (A{beta}1-40), we show that different fibril morphologies have different underlying molecular structures, that the predominant structure can be controlled by subtle variations in fibril growth conditions, and that both morphology and molecular structure are self-propagating when fibrils grow from preformed seeds. Different A{beta}1-40 fibril morphologies also have significantly different toxicities in neuronal cell cultures. These results have implications for the mechanism of amyloid formation, the phenomenon of strains in prion diseases, the role of amyloid fibrils in amyloid diseases, and the development of amyloid-based nano-materials. 10.1126/science.1105850}, author = {Petkova, Aneta T. and Leapman, Richard D. and Guo, Zhihong and Yau, Wai-Ming and Mattson, Mark P. and Tycko, Robert}, citeulike-article-id = {2537735}, citeulike-linkout-0 = {http://dx.doi.org/10.1126/science.1105850}, citeulike-linkout-1 = {http://www.sciencemag.org/cgi/content/abstract/307/5707/262}, citeulike-linkout-2 = {http://view.ncbi.nlm.nih.gov/pubmed/15653506}, citeulike-linkout-3 = {http://www.hubmed.org/display.cgi?uids=15653506}, day = {14}, doi = {10.1126/science.1105850}, journal = {Science}, keywords = {amyloid, simon}, month = {January}, number = {5707}, pages = {262--265}, posted-at = {2009-06-25 16:55:14}, priority = {2}, title = {Self-Propagating, Molecular-Level Polymorphism in Alzheimer's {beta}-Amyloid Fibrils}, url = {http://dx.doi.org/10.1126/science.1105850}, volume = {307}, year = {2005} }

TY - JOUR ID - citeulike:2537735 L3 - citeulike-article-id:2537735 N2 - Amyloid fibrils commonly exhibit multiple distinct morphologies in electron microscope and atomic force microscope images, often within a single image field. By using electron microscopy and solid-state nuclear magnetic resonance measurements on fibrils formed by the 40-residue {beta}-amyloid peptide of Alzheimer's disease (A{beta}1-40), we show that different fibril morphologies have different underlying molecular structures, that the predominant structure can be controlled by subtle variations in fibril growth conditions, and that both morphology and molecular structure are self-propagating when fibrils grow from preformed seeds. Different A{beta}1-40 fibril morphologies also have significantly different toxicities in neuronal cell cultures. These results have implications for the mechanism of amyloid formation, the phenomenon of strains in prion diseases, the role of amyloid fibrils in amyloid diseases, and the development of amyloid-based nano-materials. 10.1126/science.1105850 IS - 5707 JF - Science EP - 265 TI - Self-Propagating, Molecular-Level Polymorphism in Alzheimer's {beta}-Amyloid Fibrils VL - 307 SP - 262 KW - amyloid KW - simon AU - Petkova, Aneta AU - Leapman, Richard AU - Guo, Zhihong AU - Yau, Wai-Ming AU - Mattson, Mark AU - Tycko, Robert PY - 2005/01/14/ UR - http://dx.doi.org/10.1126/science.1105850 ER -