Abstract
Aluminium and zinc are known to be the major triggering agents for aggregation of amyloid peptides leading to plaque formation in Alzheimer's disease. While zinc binding to histidine in A? (amyloid ?) fragments has been implicated as responsible for aggregation, not much information is available on the interaction of aluminium with histidine. In the NMR study of the N-terminal A? fragments, DAEFRHDSGYEV (A?12) and DAEFRHDSGYEVHHQK (A?16) presented here, the interactions of the fragments with aluminium have been investigated. Significant chemical shifts were observed for few residues near the C-terminus when aluminium chloride was titrated with A?12 and A?16 peptides. Surprisingly, it is nonhistidine residues which seem to be involved in aluminium binding. Based on NMR constrained structure obtained by molecular modelling, aluminium-binding pockets in A?12 were around charged residues such as Asp, Glu. The results are discussed in terms of native structure propagation, and the relevance of histidine residues in the sequences for metal-binding interactions. We expect that the study of such short amyloid peptide fragments will not only provide clues for plaque formation in aggregated conditions but also facilitate design of potential drugs for these targets.
[NMR paper] Higher Order Amyloid Fibril Structure by MAS NMR and DNP Spectroscopy.
Higher Order Amyloid Fibril Structure by MAS NMR and DNP Spectroscopy.
Related Articles Higher Order Amyloid Fibril Structure by MAS NMR and DNP Spectroscopy.
J Am Chem Soc. 2013 Dec 4;
Authors: Debelouchina GT, Bayro MJ, Fitzpatrick AW, Ladizhansky V, Colvin MT, Caporini MA, Jaroniec CP, Bajaj VS, Rosay MM, Macphee CE, Vendruscolo M, Maas WE, Dobson CM, Griffin RG
Abstract
Protein magic angle spinning (MAS) NMR spectroscopy has generated structural models of several amyloid fibril systems, thus providing valuable information regarding the...
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12-07-2013 01:00 PM
Journal Highlight: Does aluminium bind to histidine? An NMR investigation of amyloid ?12 and amyloid ?16 fragments
Journal Highlight: Does aluminium bind to histidine? An NMR investigation of amyloid ?12 and amyloid ?16 fragments
http://www.spectroscopynow.com/common/images/thumbnails/13f9ef04f37.jpgIn an NMR study of the N-terminal amyloid peptide fragments A?12 and (A?16), non-histidine residues were found to be involved in aluminium binding.
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07-02-2013 10:20 PM
[NMR paper] NMR characterization of theinteraction of GroEL with amyloid ? as a model ligand.
NMR characterization of theinteraction of GroEL with amyloid ? as a model ligand.
Related Articles NMR characterization of theinteraction of GroEL with amyloid ? as a model ligand.
FEBS Lett. 2013 Apr 18;
Authors: Yagi-Utsumi M, Kunihara T, Nakamura T, Uekusa Y, Makabe K, Kuwajima K, Kato K
Abstract
Here we report an NMR study on the substrate interaction modes of GroEL using amyloid?(A?) as a model ligand. We found that GroEL could suppress A?(1-40) amyloid formation by interacting with its two hydrophobic segments Leu17-Ala21 and...
Solid-state NMR of amyloid membrane interactions.
Solid-state NMR of amyloid membrane interactions.
Solid-state NMR of amyloid membrane interactions.
Methods Mol Biol. 2011;752:165-77
Authors: Gehman JD, Separovic F
Solid-state NMR pulse sequences often feature fewer pulses and delays than the more common solution NMR experiments. This ostensible simplicity, however, belies the care with which experimental parameters must be determined, as solid-state NMR can be much less forgiving of improper experimental set-up. This is especially true of "semi-solid" samples, such as the phospholipid vesicles...
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06-30-2011 01:24 PM
Solid-State NMR Studies of Amyloid Fibril Structure.
Solid-State NMR Studies of Amyloid Fibril Structure.
Solid-State NMR Studies of Amyloid Fibril Structure.
Annu Rev Phys Chem. 2010 Apr 2;
Authors: Tycko R
Current interest in amyloid fibrils stems from their involvement in neurodegenerative and other diseases and from their role as an alternative structural state for many peptides and proteins. Solid-state nuclear magnetic resonance (NMR) methods have the unique capability of providing detailed structural constraints for amyloid fibrils, sufficient for the development of full molecular models. In...
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01-12-2011 11:11 AM
[NMR paper] An NMR-based quenched hydrogen exchange investigation of model amyloid fibrils formed
An NMR-based quenched hydrogen exchange investigation of model amyloid fibrils formed by cold shock protein A.
Related Articles An NMR-based quenched hydrogen exchange investigation of model amyloid fibrils formed by cold shock protein A.
Pac Symp Biocomput. 2001;:67-78
Authors: Alexandrescu AT
Acid-denatured cold shock protein A (CspA) self-assembles into polymers with properties typical of amyloid fibrils. In the present work, a quenched hydrogen exchange experiment was used to probe the interactions of CspA fibrils with solvent. Exchange...
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11-19-2010 08:32 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
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/qGRhA6CtOVc
Does aluminium bind to histidine? An NMR investigation of amyloid ?12 and amyloid ?16 fragments.
Linear Mode
