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Issue 43, 2018
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Ring structure modifications of phenylalanine 19 increase fibrillation kinetics and reduce toxicity of amyloid β (1–40)

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Abstract

We investigated the influence of the chemical structure of the phenylalanine side chain in position 19 of the 40 residue amyloid β peptide. Side chain modifications in this position yielded fibrils of essentially unaltered morphology, structure, and dynamics, but significantly increased fibrillation kinetics and diminished the toxicity of the peptides.

Graphical abstract: Ring structure modifications of phenylalanine 19 increase fibrillation kinetics and reduce toxicity of amyloid β (1–40)

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Publication details

The article was received on 02 Mar 2018, accepted on 01 May 2018 and first published on 03 May 2018


Article type: Communication
DOI: 10.1039/C8CC01733F
Citation: Chem. Commun., 2018,54, 5430-5433

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    Ring structure modifications of phenylalanine 19 increase fibrillation kinetics and reduce toxicity of amyloid β (1–40)

    A. Korn, D. Surendran, M. Krueger, S. Maiti and D. Huster, Chem. Commun., 2018, 54, 5430
    DOI: 10.1039/C8CC01733F

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