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

    Research output: Contribution to journalArticle

    36 Citations (Scopus)

    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 languageEnglish (US)
    Pages (from-to)1835-1839
    Number of pages5
    JournalBioorganic and Medicinal Chemistry Letters
    Volume18
    Issue number6
    DOIs
    StatePublished - Mar 15 2008

    Fingerprint

    Nucleotide Aptamers
    Single-Stranded DNA
    Transforming Growth Factors
    Proteins
    Phosphates
    In Vitro Techniques

    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 journalArticle

    Kang, Jonghoon ; Lee, Myung Soog ; Copland, John A. ; Luxon, Bruce A. ; Gorenstein, David G. / Combinatorial selection of a single stranded DNA thioaptamer targeting TGF-β1 protein. In: Bioorganic and Medicinal Chemistry Letters. 2008 ; Vol. 18, No. 6. pp. 1835-1839.
    @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 = "3",
    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

    VL - 18

    SP - 1835

    EP - 1839

    JO - Bioorganic and Medicinal Chemistry Letters

    JF - Bioorganic and Medicinal Chemistry Letters

    SN - 0960-894X

    IS - 6

    ER -