Evolution of a histone H4-K16 acetyl-specific DNA aptamer

Berea A R Williams; Liyun Lin; Stuart Lindsay; John C. Chaput

doi:10.1021/ja900916p

Evolution of a histone H4-K16 acetyl-specific DNA aptamer

Berea A R Williams, Liyun Lin, Stuart Lindsay, John C. Chaput

Research output: Contribution to journal › Article › peer-review

46 Scopus citations

Abstract

We report the in vitro selection of DNA aptamers that bind to histone H4 proteins acetylated at lysine 16. The best aptamer identified in this selection binds to the target protein with a K _d of 21 nM and discriminates against both the nonacetylated protein and histone H4 proteins acetylated at lysine 8. Comparative binding assays performed with a chip-quality antibody reveal that this aptamer binds to the acetylated histone target with similar affinity to a commercial antibody but shows significantly greater specificity (15-fold versus 2400-fold) for the target molecule. This result demonstrates that aptamers that are both modification and location specific can be generated to bind specific protein post-translational modifications.

Original language	English (US)
Pages (from-to)	6330-6331
Number of pages	2
Journal	Journal of the American Chemical Society
Volume	131
Issue number	18
DOIs	https://doi.org/10.1021/ja900916p
State	Published - May 13 2009

ASJC Scopus subject areas

Catalysis
General Chemistry
Biochemistry
Colloid and Surface Chemistry

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Evolution of a histone H4-K16 acetyl-specific DNA aptamer

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