Related ArticlesBinding Modes of Thioflavin T on the Surface of Amyloid Fibrils by NMR.
Chemphyschem. 2016 May 11;
Authors: Ivancic V, Ekanayake O, Lazo N
Abstract
The mechanism for the interaction of thioflavin T (ThT) with amyloid fibrils at the molecular level is not known. Here, we used ¹H NMR spectroscopy to determine the binding mode of ThT on the surface of fibrils from lysozyme and insulin. Relayed rotating-frame Overhauser enhancements in ThT were observed indicating that the orientation of ThT is orthogonal to the fibril surface. Importantly, the assembly state of ThT on both surfaces is different. On the surface of insulin fibrils, ThT is oligomeric as indicated by rapid ¹H spin-lattice relaxation rate in the rotating frame (R??) presumably due to intermolecular dipole-dipole interactions between ThT molecules. In contrast, ThT on the surface of lysozyme fibrils is a monomer as indicated by slower ¹H R??. These results shed new light into the mechanism for the enhancement of ThT fluorescence and may lead to more efficient detectors of amyloid assemblies which have escaped detection by ThT in monomer form.
PMID: 27165642 [PubMed - as supplied by publisher]
[NMR paper] Quenched Hydrogen Exchange NMR of Amyloid Fibrils.
Quenched Hydrogen Exchange NMR of Amyloid Fibrils.
Related Articles Quenched Hydrogen Exchange NMR of Amyloid Fibrils.
Methods Mol Biol. 2016;1345:211-22
Authors: Alexandrescu AT
Abstract
Amyloid fibrils are associated with a number of human diseases. These aggregatively misfolded intermolecular ?-sheet assemblies constitute some of the most challenging targets in structural biology because to their complexity, size, and insolubility. Here, protocols and controls are described for experiments designed to study hydrogen-bonding in...
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[NMR paper] High Resolution Structural Characterization of A?42 Amyloid Fibrils by MAS NMR.
High Resolution Structural Characterization of A?42 Amyloid Fibrils by MAS NMR.
High Resolution Structural Characterization of A?42 Amyloid Fibrils by MAS NMR.
J Am Chem Soc. 2015 May 22;
Authors: Colvin MT, Silvers R, Frohm B, Su Y, Linse S, Griffin RG
Abstract
The presence of amyloid plaques composed of amyloid beta (A?) fibrils is a hallmark of Alzheimer's disease (AD). The A? peptide is present as several length variants with two common alloforms consisting of 40 and 42 amino acids, denoted A?1-40 and A?1-42, respectively....
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05-23-2015 10:08 AM
[NMR paper] Capturing a reactive state of amyloid aggregates: NMR-based characterization of copper-bound Alzheimer disease amyloid ?-fibrils in a redox cycle.
Capturing a reactive state of amyloid aggregates: NMR-based characterization of copper-bound Alzheimer disease amyloid ?-fibrils in a redox cycle.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_final.gif Related Articles Capturing a reactive state of amyloid aggregates: NMR-based characterization of copper-bound Alzheimer disease amyloid ?-fibrils in a redox cycle.
J Biol Chem. 2014 Apr 4;289(14):9998-10010
Authors: Parthasarathy S, Yoo B, McElheny D, Tay W,...
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05-31-2014 01:57 PM
Molecular-Level Examination of Cu2+ Binding Structure for Amyloid Fibrils of 40-Residue Alzheimer’s ? by Solid-State NMR Spectroscopy
Molecular-Level Examination of Cu2+ Binding Structure for Amyloid Fibrils of 40-Residue Alzheimer’s ? by Solid-State NMR Spectroscopy
Sudhakar Parthasarathy, Fei Long, Yifat Miller, Yiling Xiao, Dan McElheny, Kent Thurber, Buyong Ma, Ruth Nussinov and Yoshitaka Ishii
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja1072178/aop/images/medium/ja-2010-072178_0006.gif
Journal of the American Chemical Society
DOI: 10.1021/ja1072178
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA ...
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02-22-2011 11:06 PM
Probing water-accessibility in HET-s(218-289) amyloid fibrils by solid-state NMR.
Probing water-accessibility in HET-s(218-289) amyloid fibrils by solid-state NMR.
Probing water-accessibility in HET-s(218-289) amyloid fibrils by solid-state NMR.
J Mol Biol. 2010 Nov 18;
Authors: Van Melckebeke H, Schanda P, Gath J, Wasmer C, Verel R, Lange A, Meier BH, Böckmann A
Despite its importance in the context of conformational diseases, structural information is still sparse for protein fibrils. Hydrogen/deuterium exchange measurements of backbone amides allow to identify hydrogen-bonding patterns and reveal pertinent information about...
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11-26-2010 05:32 PM
Accurate Determination of Interstrand Distances and Alignment in Amyloid Fibrils by M
Accurate Determination of Interstrand Distances and Alignment in Amyloid Fibrils by Magic Angle Spinning NMR.
Related Articles Accurate Determination of Interstrand Distances and Alignment in Amyloid Fibrils by Magic Angle Spinning NMR.
J Phys Chem B. 2010 Oct 6;
Authors: Caporini MA, Bajaj VS, Veshtort M, Fitzpatrick A, Macphee CE, Vendruscolo M, Dobson CM, Griffin RG
Amyloid fibrils are structurally ordered aggregates of proteins whose formation is associated with many neurodegenerative and other diseases. For that reason, their high-resolution...
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10-12-2010 02:52 PM
Atomic-Resolution Three-Dimensional Structure of HET-s(218-289) Amyloid Fibrils by So
Atomic-Resolution Three-Dimensional Structure of HET-s(218-289) Amyloid Fibrils by Solid-State NMR Spectroscopy
He?le?ne Van Melckebeke, Christian Wasmer, Adam Lange, Eiso AB, Antoine Loquet, Anja Bo?ckmann and Beat H. Meier
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja104213j/aop/images/medium/ja-2010-04213j_0001.gif
Journal of the American Chemical Society
DOI: 10.1021/ja104213j
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http://feeds.feedburner.com/~r/acs/jacsat/~4/qGRhA6CtOVc
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High-Resolution MAS NMR Analysis of PI3-SH3 Amyloid Fibrils: Backbone Conformation an
High-Resolution MAS NMR Analysis of PI3-SH3 Amyloid Fibrils: Backbone Conformation and Implications for Protofilament Assembly and Structure
http://pubs.acs.org//appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi100864t/aop/images/medium/bi-2010-00864t_0004.gifBiochemistry, Volume 0, Issue 0, Articles ASAP (As Soon As Publishable).
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Binding Modes of Thioflavin T on the Surface of Amyloid Fibrils by NMR.
Linear Mode
