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Issue 83, 2018
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Self-assembly of penta-selenopeptides into amyloid fibrils

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Here, we report the synthesis of a penta-selenopeptide consisting of five benzyl protected selenocysteine residues. This selenopeptide was well characterized by both one- and two-dimensional (D) NMR spectroscopies. We find that the solution conformation is enriched with β-sheet structures, which have a propensity to self-assemble and form amyloid fibrils.

Graphical abstract: Self-assembly of penta-selenopeptides into amyloid fibrils

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Publication details

The article was received on 10 Aug 2018, accepted on 13 Sep 2018 and first published on 14 Sep 2018

Article type: Communication
DOI: 10.1039/C8CC06528D
Citation: Chem. Commun., 2018,54, 11697-11700

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    Self-assembly of penta-selenopeptides into amyloid fibrils

    R. P. Gokula, J. Mahato, H. B. Singh and A. Chowdhury, Chem. Commun., 2018, 54, 11697
    DOI: 10.1039/C8CC06528D

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