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

Cancer Biology

Research output: Contribution to journal › Article › peer-review

44 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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10.1016/j.bmcl.2008.02.023

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title = "Combinatorial selection of a single stranded DNA thioaptamer targeting TGF-β1 protein",

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.",

keywords = "Aptamer, Chemiluminescence, Entropy, Phosphorothioate, Selection, Thioaptamer, Transforming growth factor-β1",

author = "Jonghoon Kang and Lee, {Myung Soog} and Copland, {John A.} and Luxon, {Bruce A.} and Gorenstein, {David G.}",

note = "Funding Information: This work was supported by grants from the U.S. Edgewood Chemical Biological Center (W911 SR-04-C-0065), NIH (Grants AI27744 and U01 AI054827), NIEHS (Grant ES06676), NHLBI (Grant N01HV28184), the Welch Foundation (Grant H1296) and NIH/NCI (R01CA104505 to J.A.C.). ",

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doi = "10.1016/j.bmcl.2008.02.023",

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AU - Kang, Jonghoon

AU - Lee, Myung Soog

AU - Copland, John A.

AU - Luxon, Bruce A.

AU - Gorenstein, David G.

N1 - Funding Information: This work was supported by grants from the U.S. Edgewood Chemical Biological Center (W911 SR-04-C-0065), NIH (Grants AI27744 and U01 AI054827), NIEHS (Grant ES06676), NHLBI (Grant N01HV28184), the Welch Foundation (Grant H1296) and NIH/NCI (R01CA104505 to J.A.C.).

PY - 2008/3/15

Y1 - 2008/3/15

N2 - 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.

AB - 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.

KW - Aptamer

KW - Chemiluminescence

KW - Entropy

KW - Phosphorothioate

KW - Selection

KW - Thioaptamer

KW - Transforming growth factor-β1

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

Abstract

Keywords

ASJC Scopus subject areas

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