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GeNMR
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Default NMR structure of the water soluble A?17-34 peptide.

NMR structure of the water soluble A?17-34 peptide.

Related Articles NMR structure of the water soluble A?17-34 peptide.

Biosci Rep. 2014 Oct 6;

Authors: Fonar G, Samson AO

Abstract
Alzheimer's disease is the most common neurodegenerative disorder in the world. Its most significant symptoms are memory loss and decrease in cognition. Alzheimer's disease is characterized by aggregation of two proteins in the brain namely amyloid ? (A?) and tau. Recent evidence suggests that the interaction of soluble A? with nicotinic acetylcholine receptors (nAChR) contributes to disease progression. In this study, we determine the nuclear magnetic resonance (NMR) structure of an A?17-34 peptide solubilized by the addition of two glutamic acids at each terminus. Our results indicate that the A? peptide adopts an ?-helical structure for residues 19-26 and 28-33. The ?-helical structure is broken around residues S26, N27, and K28, which form a kink in the helical conformation. This ?-helix was not described earlier in an aqueous solution without organic solvents, and at physiological conditions (pH 7). These data are in agreement with A? adopting an ?-helical conformation in the membrane before polymerizing into amyloid ?-sheets and provide insight into the intermediate state of A? in Alzheimer's disease.


PMID: 25284368 [PubMed - as supplied by publisher]



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