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

文献情報

出版日 2006-08-30

DOI 10.1039/B607657B

インパクトファクター 6.222

著者

Sudipta Ray, Apurba K. Das, Michael G. B. Drew, Arindam Banerjee

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要旨

A water-soluble tripeptide Val–Ile–Ala (VIA) 1, bearing sequence identity with the C-terminal portion of the Alzheimer Aβ-peptide (Aβ40–42), self-assembles, in crystalline form, to produce an intermolecularly hydrogen bonded supramolecular β-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 β-sheet structure that forms branched nanofibrils which do not show any characteristic features of amyloid-like fibrils.

掲載誌

Chemical Communications

CiteScore: 8.6

自己引用率: 4.7%

年間論文数: 2458

ChemComm publishes urgent research which is of outstanding significance and interest to experts in the field, while also appealing to the journal’s broad chemistry readership. Our communication format is ideally suited to short, urgent studies that are of such importance that they require accelerated publication. Our scope covers all topics in chemistry, and research at the interface of chemistry and other disciplines (such as materials science, nanoscience, physics, engineering and biology) where there is a significant novelty in the chemistry aspects. Major topic areas covered include: Analytical Chemistry Catalysis Chemical Biology and medicinal chemistry Computational Chemistry and Machine Learning Energy and sustainable chemistry Environmental Chemistry Green Chemistry Inorganic Chemistry Materials Chemistry Nanoscience Organic Chemistry Physical Chemistry Polymer Chemistry Supramolecular Chemistry

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

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