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 | |
| State | Published - Mar 15 2008 |
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Keywords
- Aptamer
- Chemiluminescence
- Entropy
- Phosphorothioate
- Selection
- Thioaptamer
- Transforming growth factor-β1
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Organic Chemistry
- Drug Discovery
- Pharmaceutical Science
Cite this
Combinatorial selection of a single stranded DNA thioaptamer targeting TGF-β1 protein. / Kang, Jonghoon; Lee, Myung Soog; Copland, John A.; Luxon, Bruce A.; Gorenstein, David G.
In: Bioorganic and Medicinal Chemistry Letters, Vol. 18, No. 6, 15.03.2008, p. 1835-1839.Research output: Contribution to journal › Article
}
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
VL - 18
SP - 1835
EP - 1839
JO - Bioorganic and Medicinal Chemistry Letters
JF - Bioorganic and Medicinal Chemistry Letters
SN - 0960-894X
IS - 6
ER -