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Journal of Biomedical Optics • Open Access

Fluorescence lifetime dynamics of enhanced green fluorescent protein in protein aggregates with expanded polyglutamine
Author(s): Vladimir Ghukasyan; Chih-Chun Hsu; Chia-Rung Liu; Fu-Jen Kao; Tzhu-Hao Cheng

Paper 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.

Paper Details

Date Published: 1 January 2010
PDF: 11 pages
J. Biomed. Opt. 15(1) 016008 doi: 10.1117/1.3290821
Published in: Journal of Biomedical Optics Volume 15, Issue 1
Show Author Affiliations
Vladimir Ghukasyan, National Yang-Ming Univ. (Taiwan)
Chih-Chun Hsu, National Yang-Ming Univ. (Taiwan)
Chia-Rung Liu, National Yang-Ming Univ. (Taiwan)
Fu-Jen Kao, National Yang-Ming Univ. (Taiwan)
Tzhu-Hao Cheng, National Yang-Ming Univ. (Taiwan)

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