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PMID: 21338068 Published · ppublish English Journal Article Research Support, N.I.H., Intramural

Residue-specific fluorescent probes of α-synuclein: detection of early events at the N- and C-termini during fibril assembly.

Biochemistry ·Vol. 50 ·No. 12 ·2011-03-29 ·Pages 1963-5

Yap TL, Pfefferkorn CM, Lee JC

Abstract

In the Parkinson's disease-associated state, α-synuclein undergoes large conformational changes, forming ordered, β-sheet-containing fibrils. To unravel the role of specific residues during the fibril assembly process, we prepared single-Cys mutants in the disordered (G7C and Y136C) and proximal (V26C and L100C) fibril core sites and derivatized them with environmentally sensitive dansyl (Dns) fluorophores. Dns fluorescence exhibits residue specificity in spectroscopic properties as well as kinetic behavior; early kinetic events were revealed by probes located at positions 7 and 136 compared to those at positions 26 and 100.

MeSH Terms
Amyloid/chemistry,genetics,metabolism Dansyl Compounds/chemistry Fluorescent Dyes/chemistry Humans Mutation Parkinson Disease/metabolism Protein Multimerization Protein Structure, Secondary Spectrometry, Fluorescence Substrate Specificity alpha-Synuclein/chemistry,genetics,metabolism
Chemicals
Amyloid Dansyl Compounds Fluorescent Dyes alpha-Synuclein
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Yap Thai Leong
Laboratory of Molecular Biophysics, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892, United States.
Pfefferkorn Candace M
Lee Jennifer C
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Article Info
Journal
Biochemistry
Abbr.
Biochemistry
ISSN
1520-4995
Published
2011-03-29
Epub
2011-00-21
Pages
1963-5
Language
English
Region
United States
NLM ID
0370623
PMCID
PMC3074234
Subset
IM
Grants
Intramural NIH HHS · ZIA HL001055-04 · United States
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