Fluorescence lifetime dynamics of enhanced green fluorescent protein in protein aggregates with expanded polyglutamine

Vladimir Ghukasyan, Chih Chun Hsu, Chia Rung Liu, Fu Jen Kao, Tzu Hao Cheng*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

20 Scopus citations

Abstract

Protein aggregation is one of the characteristic steps in a number of neurodegenerative diseases eventually leading to neuronal death and thorough study of aggregation is required for the development of effective therapy. We apply fluorescence lifetime imaging for the characterization of the fluorescence dynamics of the enhanced green fluorescent protein (eGFP) in fusion with the polyQ-expanded polyglutamine stretch. At the expansion of polyQ above 39 residues, it has an inherent propensity to form amyloid-like fibrils and aggregates, and is responsible for Huntington's disease. The results of the experiments show that expression of the eGFP in fusion with the 97Q protein leads to the decrease of the eGFP fluorescence lifetime by ∼ 300 ps. This phenomenon does not appear in Hsp104-deficient cells, where the aggregation in polyQ is prevented. We demonstrate that the lifetime decrease observed is related to the aggregation per se and discuss the possible role of refractive index and homo-FRET in these dynamics.

Original languageEnglish
Article number016008
JournalJournal of Biomedical Optics
Volume15
Issue number1
DOIs
StatePublished - 2010

Keywords

  • Aggregation
  • Enhanced green fluorescent protein
  • Fluorescence anisotropy imaging
  • Fluorescence lifetime imaging
  • Förster resonance energy transfer
  • Homo-FRET
  • Polyglutamine
  • Refractive index

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