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

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 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

Access to Document

10.1016/j.bmcl.2008.02.023

Fingerprint Dive into the research topics of 'Combinatorial selection of a single stranded DNA thioaptamer targeting TGF-β1 protein'. Together they form a unique fingerprint.

Cite this

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

@article{8cba0b3f6e3942cfa5df0d0125bd1636,

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.}",

year = "2008",

month = mar,

day = "15",

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

language = "English (US)",

volume = "18",

pages = "1835--1839",

journal = "Bioorganic and Medicinal Chemistry Letters",

issn = "0960-894X",

publisher = "Elsevier Limited",

number = "6",

}

TY - JOUR

T1 - Combinatorial selection of a single stranded DNA thioaptamer targeting TGF-β1 protein

AU - Kang, Jonghoon

AU - Lee, Myung Soog

AU - Copland, John A.

AU - Luxon, Bruce A.

AU - Gorenstein, David G.

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

UR - http://www.scopus.com/inward/record.url?scp=40749129242&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=40749129242&partnerID=8YFLogxK

U2 - 10.1016/j.bmcl.2008.02.023

DO - 10.1016/j.bmcl.2008.02.023

M3 - Article

C2 - 18294846

AN - SCOPUS:40749129242

VL - 18

SP - 1835

EP - 1839

JO - Bioorganic and Medicinal Chemistry Letters

JF - Bioorganic and Medicinal Chemistry Letters

SN - 0960-894X

IS - 6

ER -