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Studies of Interaction Between Cyanine Dye T-284 and Fibrillar Alpha-Synuclein
- Source :
- Journal of Fluorescence, 20(6), 1267-74. Springer New York, Journal of fluorescence, 20(6), 1267-1274. Springer, Volkova, K D, Kovalska, V B, Yu Losytskyy, M, Veldhuis, G, Segers-Nolten, G M J, Tolmachev, O I, Subramaniam, V & Yarmoluk, S M 2010, ' Studies of interaction between cyanine dye T-284 and fibrillar alpha-synuclein ', Journal of Fluorescence, vol. 20, no. 6, pp. 1267-74 . https://doi.org/10.1007/s10895-010-0678-1
- Publication Year :
- 2010
- Publisher :
- Springer Science and Business Media LLC, 2010.
-
Abstract
- A key feature of Parkinson's disease is the formation and accumulation of amyloid fibrils of the natively unfolded protein α-synuclein (ASN) inside neurons. Recently we have proposed novel sensitive monomethinecyanine dye T-284 as fluorescent probe for quantitative detection of ASN amyloid fibrils. In this study the T-284 dye complex with ASN fibril was characterized by means of fluorescence anisotropy, atomic force microscopy and time-resolved fluorescence techniques to give further insights into the mode of dye interaction with amyloid fibrils. The fluorescence anisotropy of T-284 was shown to noticeably increase upon addition of aggregated proteins indicating on stable dye/amyloid fibril complex formation. AFM imaging of fibrillar wild-type ASN revealed differences in heights between ASN fibrils alone and in presence of the T-284 dye (6.37 ± 1.0 nm and 8.0 ± 1.1 nm respectively), that is believed to be caused by embedding of T-284 dye molecules in the "binding channel" running along the fibril. Fluorescence decay analysis of the T-284 in complexes with fibrillar ASN variants revealed the fluorescence lifetime values for T-284/fibril complexes to be an order of magnitude higher as compared to the free dye. Also, the fluorescence decay of free T-284 was bi-exponential, while dye bound to protein yields tri-exponential decay. We suppose that in complexes with fibrillar ASN variants T-284 dye might exist in different "populations" due to interaction with fibrils in different conformers and ways. The exact binding mode of T-284 with ASN fibrils needs further studies. Studied parameters of dye/amyloid fibril complexes are important for the characterization and screening of newly-developed amyloid-sensitive dyes.
- Subjects :
- Sociology and Political Science
Clinical Biochemistry
Fluorescence Polarization
macromolecular substances
Microscopy, Atomic Force
Research Support
Fibril
Biochemistry
METIS-268279
chemistry.chemical_compound
Journal Article
Molecule
Cyanine
Non-U.S. Gov't
Conformational isomerism
Spectroscopy
Fluorescent Dyes
Cyanine dyes - α-synuclein - Amyloid fibrils - Fluorescent detection - Atomic force microscopy
Alpha-synuclein
Microscopy
Molecular Structure
Atomic force microscopy
Research Support, Non-U.S. Gov't
Atomic Force
Carbocyanines
Fluorescence
IR-77901
Clinical Psychology
Crystallography
chemistry
alpha-Synuclein
Law
Social Sciences (miscellaneous)
Fluorescence anisotropy
Subjects
Details
- ISSN :
- 15734994 and 10530509
- Volume :
- 20
- Database :
- OpenAIRE
- Journal :
- Journal of Fluorescence
- Accession number :
- edsair.doi.dedup.....77bd58becae6d8606586353d3155cc49