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Self-assembly of penta-selenopeptide into amyloid fibrils

Abstract

Here, we report the synthesis of penta-selenopeptide comprising of five benzyl protected selenocysteine residues. This selenopeptide was well characterized by both one and two-dimensional (D) NMR spectroscopy. We find that the solution conformation is enriched with -sheet structure, which has propensity to self-assemble and form 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, Accepted Manuscript
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    Self-assembly of penta-selenopeptide into amyloid fibrils

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

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