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

doi:10.1016/j.bmcl.2008.02.023

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

Biochemistry & Molecular Biology

Research output: Contribution to journal › Article

41 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 language	English (US)
Pages (from-to)	1835-1839
Number of pages	5
Journal	Bioorganic and Medicinal Chemistry Letters
Volume	18
Issue number	6
DOIs	https://doi.org/10.1016/j.bmcl.2008.02.023
State	Published - 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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Kang, J., Lee, M. S., Copland, J. A., Luxon, B. A., & Gorenstein, D. G. (2008). Combinatorial selection of a single stranded DNA thioaptamer targeting TGF-β1 protein. Bioorganic and Medicinal Chemistry Letters, 18(6), 1835-1839. https://doi.org/10.1016/j.bmcl.2008.02.023

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AU - Luxon, Bruce A.

AU - Gorenstein, David G.

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KW - Selection

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KW - Transforming growth factor-β1

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