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A short water-soluble self-assembling peptide forms amyloid-like fibrils

Ray, S., Das, A.K., Drew, M.G.B. and Banerjee, A. (2006) A short water-soluble self-assembling peptide forms amyloid-like fibrils. Chemical Communications (40). pp. 4230-4232. ISSN 1359-7345

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To link to this item DOI: 10.1039/b607657b

Abstract/Summary

A water-soluble tripeptide Val-Ile-Ala (VIA) 1, bearing sequence identity with the C-terminal portion of the Alzheimer A beta-peptide (A beta(40-42)), self-assembles, in crystalline form, to produce an intermolecularly hydrogen bonded supramolecular beta-sheet structure which self-associates to form straight, unbranched nanofibrils exhibiting amyloid-like behavior; in contrast, the synthetic tripeptide Ala-Val-Ile (AVI) 2 self-assembles to produce a beta-sheet structure that forms branched nanofibrils which do not show any characteristic features of amyloid-like fibrils.

Item Type:Article
Refereed:Yes
Divisions:Faculty of Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
ID Code:11579
Uncontrolled Keywords:ALZHEIMERS-DISEASE, BETA-SHEET, STRUCTURAL MODEL, ANTIPARALLEL, PROTEIN, PARALLEL, BETA-AMYLOID((10-35)), ALIGNMENT, RESIDUES

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