Molecular-Level Insights into Amyloid Polymorphism from Solid-State Nuclear Magnetic Resonance
作者： Robert Tycko
DOI: 10.1016/B978-0-12-394431-3.00004-3
关键词: Solid-state nuclear magnetic resonance 、 Polymorphism (materials science) 、 Amino acid 、 Globular protein 、 Intermolecular force 、 Prion protein 、 Chemistry 、 Crystallography 、 Fibril 、 Molecular level
摘要: Abstract Although the molecular structures of globular proteins are determined uniquely by their amino acid sequences, same is not true amyloid fibrils. Solid-state nuclear magnetic resonance (NMR) measurements have been especially important in elucidating and structural variations within fibrils because these provide detailed site-specific information about conformations intermolecular associations, without requiring crystallinity or solubility. This chapter discusses several examples which solid-state NMR has used to develop full models for characterize molecular-level that underlie polymorphism. The include selected results 40-residue β-amyloid (Aβ1-40) fibrils, formed a disease-associated Aβ1-40 mutant, 15-residue fragment Aβ1-40, yeast prion protein Ure2p.
sci-hub.se 参考文章(49)
Ivano Bertini, Leonardo Gonnelli, Claudio Luchinat, Jiafei Mao, Antonella Nesi, A new structural model of Aβ40 fibrils. Journal of the American Chemical Society. ,vol. 133, pp. 16013- 16022 ,(2011) , 10.1021/JA2035859
Robert Tycko, Kimberly L. Sciarretta, Joseph P. R. O. Orgel, Stephen C. Meredith, Evidence for Novel β-Sheet Structures in Iowa Mutant β-Amyloid Fibrils Biochemistry. ,vol. 48, pp. 6072- 6084 ,(2009) , 10.1021/BI9002666
J.-P. Colletier, A. Laganowsky, M. Landau, M. Zhao, A. B. Soriaga, L. Goldschmidt, D. Flot, D. Cascio, M. R. Sawaya, D. Eisenberg, Molecular basis for amyloid-beta polymorphism. Proceedings of the National Academy of Sciences of the United States of America. ,vol. 108, pp. 16938- 16943 ,(2011) , 10.1073/PNAS.1112600108
T. L. S. Benzinger, D. M. Gregory, T. S. Burkoth, H. Miller-Auer, D. G. Lynn, R. E. Botto, S. C. Meredith, Propagating structure of Alzheimer’s β-amyloid(10–35) is parallel β-sheet with residues in exact register Proceedings of the National Academy of Sciences of the United States of America. ,vol. 95, pp. 13407- 13412 ,(1998) , 10.1073/PNAS.95.23.13407
Robert Tycko, Symmetry-based constant-time homonuclear dipolar recoupling in solid state NMR. Journal of Chemical Physics. ,vol. 126, pp. 064506- 064506 ,(2007) , 10.1063/1.2437194
Claire S. Goldsbury, Sabine Wirtz, Shirley A. Müller, Shabir Sunderji, Peter Wicki, Ueli Aebi, Peter Frey, Studies on the in Vitro Assembly of Aβ 1–40: Implications for the Search for Aβ Fibril Formation Inhibitors Journal of Structural Biology. ,vol. 130, pp. 217- 231 ,(2000) , 10.1006/JSBI.2000.4259
Robert Tycko, Yoshitaka Ishii, Constraints on supramolecular structure in amyloid fibrils from two-dimensional solid-state NMR spectroscopy with uniform isotopic labeling. Journal of the American Chemical Society. ,vol. 125, pp. 6606- 6607 ,(2003) , 10.1021/JA0342042
Jessica Meinhardt, Carsten Sachse, Peter Hortschansky, Nikolaus Grigorieff, Marcus Fändrich, Aβ(1-40) Fibril Polymorphism Implies Diverse Interaction Patterns in Amyloid Fibrils Journal of Molecular Biology. ,vol. 386, pp. 869- 877 ,(2009) , 10.1016/J.JMB.2008.11.005
H. Heise, W. Hoyer, S. Becker, O. C. Andronesi, D. Riedel, M. Baldus, Molecular-level secondary structure, polymorphism, and dynamics of full-length ¿-synuclein fibrils studied by solid-state NMR Proceedings of the National Academy of Sciences of the United States of America. ,vol. 102, pp. 15871- 15876 ,(2005) , 10.1073/PNAS.0506109102
F. Shewmaker, R. B. Wickner, R. Tycko, Amyloid of the prion domain of Sup35p has an in-register parallel β-sheet structure Proceedings of the National Academy of Sciences of the United States of America. ,vol. 103, pp. 19754- 19759 ,(2006) , 10.1073/PNAS.0609638103