Label transfer chemistry for the characterization of protein-protein interactions

Bo Liu; Chase T. Archer; Lyle Burdine; Thomas G. Gillette; Thomas Kodadek

doi:10.1021/ja072904r

Label transfer chemistry for the characterization of protein-protein interactions

Bo Liu, Chase T. Archer, Lyle Burdine, Thomas G. Gillette, Thomas Kodadek

Internal Medicine

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40 Scopus citations

Abstract

A new label transfer method is presented that overcomes most of the limitations of current systems. A protein of interest is tagged with a tetracysteine sequence (FlAsH receptor peptide (FRP)) that binds tightly and specifically to a chimeric molecule 3,4-dihydroxyphenylalanine-biotin-4′,5′-bis(1,3,2-dithioarsolan-2-yl)fluorescein (DOPA-biotin-FlAsH). Upon brief periodate oxidation, the DOPA moiety is cross-linked to nearby surface-exposed nucleophiles. Boiling the products in excess dithiol dissolves the FlAsH-FRP interaction, resulting in transfer of the biotin tag to the partner proteins, allowingthem to be identified by standard methods.

Original language	English (US)
Pages (from-to)	12348-12349
Number of pages	2
Journal	Journal of the American Chemical Society
Volume	129
Issue number	41
DOIs	https://doi.org/10.1021/ja072904r
State	Published - Oct 17 2007

ASJC Scopus subject areas

Catalysis
General Chemistry
Biochemistry
Colloid and Surface Chemistry

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10.1021/ja072904r

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abstract = "A new label transfer method is presented that overcomes most of the limitations of current systems. A protein of interest is tagged with a tetracysteine sequence (FlAsH receptor peptide (FRP)) that binds tightly and specifically to a chimeric molecule 3,4-dihydroxyphenylalanine-biotin-4′,5′-bis(1,3,2-dithioarsolan-2-yl)fluorescein (DOPA-biotin-FlAsH). Upon brief periodate oxidation, the DOPA moiety is cross-linked to nearby surface-exposed nucleophiles. Boiling the products in excess dithiol dissolves the FlAsH-FRP interaction, resulting in transfer of the biotin tag to the partner proteins, allowingthem to be identified by standard methods.",

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AU - Liu, Bo

AU - Archer, Chase T.

AU - Burdine, Lyle

AU - Gillette, Thomas G.

AU - Kodadek, Thomas

PY - 2007/10/17

Y1 - 2007/10/17

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AB - A new label transfer method is presented that overcomes most of the limitations of current systems. A protein of interest is tagged with a tetracysteine sequence (FlAsH receptor peptide (FRP)) that binds tightly and specifically to a chimeric molecule 3,4-dihydroxyphenylalanine-biotin-4′,5′-bis(1,3,2-dithioarsolan-2-yl)fluorescein (DOPA-biotin-FlAsH). Upon brief periodate oxidation, the DOPA moiety is cross-linked to nearby surface-exposed nucleophiles. Boiling the products in excess dithiol dissolves the FlAsH-FRP interaction, resulting in transfer of the biotin tag to the partner proteins, allowingthem to be identified by standard methods.

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Label transfer chemistry for the characterization of protein-protein interactions

Abstract

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