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.
MeSH terms
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Amyloid / chemical synthesis
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Amyloid / chemistry*
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Amyloid / ultrastructure
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Chemistry Techniques, Synthetic
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Circular Dichroism
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Microscopy, Electron, Transmission
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Peptides / chemical synthesis
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Peptides / chemistry*
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Protein Structure, Secondary
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Selenocysteine / chemical synthesis
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Selenocysteine / chemistry*
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Spectroscopy, Fourier Transform Infrared
Substances
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Amyloid
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Peptides
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Selenocysteine