Combinatorial selection of a single stranded DNA thioaptamer targeting TGF-β1 protein

Jonghoon Kang, Myung Soog Lee, John A. Copland, Bruce A. Luxon, David G. Gorenstein

Research output: Contribution to journalArticle

40 Scopus citations

Abstract

A phosphorothioate single-stranded DNA aptamer (thioaptamer) targeting transforming growth factor-β1 (TGF-β1) was isolated by in-vitro combinatorial selection. The aptamer selection procedure was designed to modify the backbone of single-stranded DNA aptamers, where 5′ of both A and C are phosphorothioates, since this provides enhanced nuclease resistance as well as higher affinity than that of a phosphate counterpart. The thioaptamer selected from a combinatorial library (5 × 1014 sequences) binds to TGF-β1 protein with an affinity of 90 nM. In this report, sequence, predicted secondary structure, and binding affinity of the selected thioaptamer (T18_1_3) are presented.

Original languageEnglish (US)
Pages (from-to)1835-1839
Number of pages5
JournalBioorganic and Medicinal Chemistry Letters
Volume18
Issue number6
DOIs
StatePublished - Mar 15 2008

Keywords

  • Aptamer
  • Chemiluminescence
  • Entropy
  • Phosphorothioate
  • Selection
  • Thioaptamer
  • Transforming growth factor-β1

ASJC Scopus subject areas

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

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