Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1376791 | Bioorganic & Medicinal Chemistry Letters | 2008 | 5 Pages |
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.
Graphical abstractWe have isolated a high affinity thioaptamer targeting TGF-β1. The ‘thio’ effect is well described by our theoretical model.Figure optionsDownload full-size imageDownload as PowerPoint slide