High-resolution temperature-concentration diagram of alpha-synuclein conformation obtained from a single Förster resonance energy transfer image in a microfluidic device

Vandelinder, Virginia, Ferreon, Allan Chris M., Gambin, Yann, Deniz, Ashok A. and Groisman, Alex (2009) High-resolution temperature-concentration diagram of alpha-synuclein conformation obtained from a single Förster resonance energy transfer image in a microfluidic device. Analytical Chemistry, 81 16: 6929-6935. doi:10.1021/ac901008c


Author Vandelinder, Virginia
Ferreon, Allan Chris M.
Gambin, Yann
Deniz, Ashok A.
Groisman, Alex
Title High-resolution temperature-concentration diagram of alpha-synuclein conformation obtained from a single Förster resonance energy transfer image in a microfluidic device
Formatted title
High-resolution temperature-concentration diagram of α-synuclein conformation obtained from a single Förster resonance energy transfer image in a microfluidic device
Journal name Analytical Chemistry   Check publisher's open access policy
ISSN 0003-2700
1520-6882
Publication date 2009-08-15
Sub-type Article (original research)
DOI 10.1021/ac901008c
Open Access Status Not yet assessed
Volume 81
Issue 16
Start page 6929
End page 6935
Total pages 7
Place of publication Washington, DC, United States
Publisher American Chemical Society
Language eng
Abstract We present a microfluidic device for rapid and efficient determination of protein conformations in a range of medium conditions and temperatures. The device generates orthogonal gradients of concentration and temperature in an interrogation area that fits into the field of view of an objective lens with a numerical aperture of 0.45. A single Forster resonance energy transfer (FRET) image of the interrogation area containing a dual-labeled protein provides a 100 × 100 point map of the FRET efficiency that corresponds to a diagram of protein conformations in the coordinates of temperature and medium conditions. The device is used to explore the conformations of α-synuclein, an intrinsically disordered protein linked to Parkinson’s and Alzheimer’s diseases, in the presence of a binding partner, the lipid-mimetic sodium dodecyl sulfate (SDS). The experiment provides a diagram of conformations of α-synuclein with 10 000 individual data points in a range of 21−47 °C and 0−2.5 mM SDS. The diagram is consistent with previous reports but also reveals new conformational transitions that would be difficult to detect with conventional techniques. The microfluidic device can potentially be used to study other biomolecular and soft-matter systems.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: ERA 2012 Admin Only
Institute for Molecular Bioscience - Publications
 
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Created: Thu, 13 Oct 2011, 22:17:46 EST by Yann Gambin on behalf of Institute for Molecular Bioscience