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 journalArticle

34 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 languageEnglish (US)
Pages (from-to)6330-6331
Number of pages2
JournalJournal of the American Chemical Society
Volume131
Issue number18
DOIs
StatePublished - May 13 2009

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

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