A four-amino acid linker between repeats in the α-synuclein sequence is important for fibril formation

Volodymyr V Shvadchak, Vinod Subramaniam

    Research output: Contribution to JournalArticleAcademicpeer-review

    Abstract

    α-Synuclein is a 140-amino acid protein that can switch conformation among intrinsically disordered in solution, helical on a membrane, and β-sheet in amyloid fibrils. Using the fluorescence of single-tryptophan mutants, we determined the immersion of different regions of the protein into lipid membranes. Our results suggest the presence of a flexible break close to residues 52-55 between two helical domains. The four-amino acid linker is not necessary for membrane binding but is important for fibril formation. A deletion mutant lacking this linker aggregates extremely slowly and slightly inhibits wild-type aggregation, possibly by blocking the growing ends of fibrils.

    Original languageEnglish
    Pages (from-to)279-81
    Number of pages3
    JournalBiochemistry
    Volume53
    Issue number2
    DOIs
    Publication statusPublished - 21 Jan 2014

    Keywords

    • Amino Acid Sequence
    • Amino Acids
    • Amyloid
    • Fluorescence
    • Humans
    • Models, Molecular
    • Mutation
    • Protein Conformation
    • Tryptophan
    • alpha-Synuclein
    • Journal Article
    • Research Support, Non-U.S. Gov't

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