Self-assembly of bivalent protein-binding agents based on oligonucleotide-linked organic fragments

K. Ingrid Sprinz, Debarati M. Tagore, Andrew D. Hamilton

Research output: Contribution to journalArticlepeer-review


A library of bidentate fragments linked through an oligonucleotide duplex was tested for binding to streptavidin. When one fragment was biotin, only biotin-containing duplexes were selected by streptavidin but when heated above the melting temperature, only bidentate biotin ligands were obtained. Thermal denaturation experiments showed that the melting temperature, thus stability, of the monodentate versus bidentate binding ligand increased from 59 to 71°C in the presence of streptavidin. Substituting biotin with 2-iminobiotin led to the exclusion of all other duplexes by the bidentate iminobiotin duplex in binding streptavidin.

Original languageEnglish (US)
Pages (from-to)3908-3911
Number of pages4
JournalBioorganic and Medicinal Chemistry Letters
Issue number17
StatePublished - Sep 1 2005


  • Bidentate
  • Combinatorial library
  • Monodentate
  • Thermal denaturation

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmaceutical Science
  • Drug Discovery
  • Clinical Biochemistry
  • Organic Chemistry


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