Issue 83, 2018

Self-assembly of penta-selenopeptides into amyloid fibrils

Abstract

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

Supplementary files

Article information

Article type
Communication
Submitted
10 Aug. 2018
Accepted
13 Sept. 2018
First published
14 Sept. 2018

Chem. Commun., 2018,54, 11697-11700

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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