Beta-amyloid oligomerisation monitored by intrinsic tyrosine fluorescence

Mariana Amaro, David J. S. Birch, Olaf J. Rolinski

Research output: Contribution to journalArticlepeer-review

42 Citations (Scopus)


Aggregation of the peptide beta-amyloid is known to be associated with Alzheimer's disease. According to recent findings the most neurotoxic aggregates are the oligomers formed in the initial stages of the aggregation process. Here we use beta-amyloid's (A beta's) intrinsic fluorophore tyrosine to probe the earliest peptide-to-peptide stages of aggregation, a region often merely labelled as a time lag, because negligible changes are observed by the commonly used probe ThT. Using spectrally resolved fluorescence decay time techniques and analysis we demonstrate how the distribution of 3 rotamer conformations of the single tyrosine in A beta tracks the aggregation across the time lag and beyond according to the initial peptide concentration. At low A beta concentrations
Original languageEnglish
Pages (from-to)6434-6441
Number of pages8
JournalPhysical Chemistry Chemical Physics
Issue number14
Publication statusPublished - 4 Mar 2011


  • protein aggregation
  • fibrils
  • peptides
  • conversion
  • fibrillation
  • Thioflavin-T
  • alpha-synuclein


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