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.
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