Transient formation of intermediate conformational states of amyloid-β peptide revealed by heteronuclear magnetic resonance spectroscopy
- 12 March 2011
- journal article
- Published by Wiley in FEBS Letters
- Vol. 585 (7), 1097-1102
- https://doi.org/10.1016/j.febslet.2011.03.014
Abstract
A detailed analysis of the NMR spectra of amyloid-β (Aβ) peptide revealed a decrease in signal intensity at higher temperature, due to a reversible conformational change of the molecule. Although peak intensity did not depend on peptide concentrations, the intensity in the region from D23 to A30 depended significantly on temperature. During the early stages of Aβ aggregation, each molecule might adopt transiently a turn conformation at around D23–A30, which converts mutually with a random coil. Stabilization of a turn by further conformational change and/or molecular association would lead to the formation of a “nucleus” for amyloid fibrilsKeywords
Funding Information
- Sankyo Foundation of Life Science
- National Center for Geriatrics and Gerontology (NCGG)
This publication has 26 references indexed in Scilit:
- Amyloid β-Protein Assembly and Alzheimer DiseasePublished by Elsevier BV ,2009
- Formation of Toxic Aβ(1–40) Fibrils on GM1 Ganglioside-Containing Membranes Mimicking Lipid Rafts: Polymorphisms in Aβ(1–40) FibrilsJournal of Molecular Biology, 2008
- Structural Classification of Toxic Amyloid OligomersJournal of Biological Chemistry, 2008
- Experimental Constraints on Quaternary Structure in Alzheimer's β-Amyloid FibrilsBiochemistry, 2005
- Self-Propagating, Molecular-Level Polymorphism in Alzheimer's ß-Amyloid FibrilsScience, 2005
- A structural model for Alzheimer's β-amyloid fibrils based on experimental constraints from solid state NMRProceedings of the National Academy of Sciences of the United States of America, 2002
- The Amyloid Hypothesis of Alzheimer's Disease: Progress and Problems on the Road to TherapeuticsScience, 2002
- MODELS OF AMYLOID SEEDING IN ALZHEIMER'S DISEASE AND SCRAPIE: Mechanistic Truths and Physiological Consequences of the Time-Dependent Solubility of Amyloid ProteinsAnnual Review of Biochemistry, 1997
- Cell Biology of the Amyloid beta-Protein Precursor and the Mechanism of Alzheimer's DiseaseAnnual Review of Cell Biology, 1994
- Seeding “one-dimensional crystallization” of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?Cell, 1993