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.
Original languageEnglish
Pages (from-to)9448-9451
Number of pages4
JournalAngewandte Chemie International Edition
Volume49
Issue number49
DOIs
Publication statusPublished - Dec 2010

Keywords

  • amyloids
  • ion mobility
  • mass spectrometry
  • oligomers
  • polypeptides
  • BETA-PROTEIN OLIGOMERIZATION
  • ION MOBILITY MEASUREMENTS
  • FIBRIL FORMATION
  • INFORMATION
  • A-BETA-42
  • CLUSTERS
  • STATES

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