Abstract
Insertion of an anthranilic acid in an amyloidogenic peptide sequence generates a novel conformationally restricted α/β-hybrid peptide that inhibits amyloid formation of Aβ(1-40) and disrupts preformed fibrillar aggregates in vitro. Such β-sheet breaker hybrid peptides (BSBHps) may be useful for designing novel physiologically important compounds relevant to diverse amyloidoses and for studying the process of aggregation.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Alzheimer Disease / metabolism
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Alzheimer Disease / pathology
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Amyloid beta-Peptides / chemical synthesis
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Amyloid beta-Peptides / chemistry
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Amyloid beta-Peptides / metabolism*
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Circular Dichroism
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Humans
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Microscopy, Electron, Transmission
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Peptide Fragments / chemical synthesis
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Peptide Fragments / chemistry
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Peptide Fragments / metabolism*
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Protein Binding
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Protein Structure, Secondary
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ortho-Aminobenzoates / chemistry
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ortho-Aminobenzoates / metabolism
Substances
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Amyloid beta-Peptides
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Peptide Fragments
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amyloid beta-protein (1-40)
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ortho-Aminobenzoates
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anthranilic acid