Characterizing early aggregates formed by an amyloidogenic peptide by mass spectrometry

Harriet L. Cole, Jason M D Kalapothakis, Guy Bennett, Perdita E. Barran, Cait E. MacPhee

    Research output: Contribution to journalArticlepeer-review

    Abstract

    What floats in the soup? Time-course and ion-mobility nano-electrospray ionization (nESI) mass spectrometry probes the early aggregation states of an amyloidogenic endecapeptide derived from amino acid residues 105-115 of the human plasma protein transthyretin. A wide range of densely packed prefibrillar oligomers 1 ≤ n ≤ 13 are observed in dynamic populations over 8 h. Copyright © 2010 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
    Original languageEnglish
    Pages (from-to)9448-9451
    Number of pages3
    JournalAngewandte Chemie - International Edition
    Volume49
    Issue number49
    DOIs
    Publication statusPublished - 3 Dec 2010

    Keywords

    • amyloids
    • ion mobility
    • mass spectrometry
    • oligomers
    • polypeptides

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