A dual-purpose synthetic colloidal platform for protease mapping: substrate profiling for Dengue and West Nile virus proteases

In a proof of concept study, we created a small focused fluorescent hexapeptide library onto 14 multiplexed barcoded sets of silica particles to probe the substrate recognition specificity of West Nile and Dengue virus proteases. A flow cytometric analysis demonstrated that the optical signature of...

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Bibliographic Details
Published in:Analytical biochemistry 2008-05, Vol.376 (1), p.151-153
Main Authors: Marcon, Lionel, Kozak, Darby, Battersby, Bronwyn J., Chappell, Keith J., Fairlie, David P., Young, Paul, Trau, Matt
Format: Article
Language:English
Subjects:
Arginine - metabolism
Dengue Virus - enzymology
Flow Cytometry
Lysine - metabolism
Peptide Hydrolases - metabolism
Peptide Library
Substrate Specificity
Viral Proteins - analysis
Viral Proteins - metabolism
West Nile virus - enzymology
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Summary:In a proof of concept study, we created a small focused fluorescent hexapeptide library onto 14 multiplexed barcoded sets of silica particles to probe the substrate recognition specificity of West Nile and Dengue virus proteases. A flow cytometric analysis demonstrated that the optical signature of each bead population remained distinguishable throughout the solid-phase peptide synthesis and proteolytic assay. As expected, both proteases displayed a narrow specificity for lysine and arginine residues in the P1 and P2 substrate positions. This open-ended platform enables the fast and simultaneous identification of peptide substrates and is applicable to other proteases.
ISSN:0003-2697
1096-0309
DOI:10.1016/j.ab.2008.01.034