| Project/Area Number |
16590082
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Drug development chemistry
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| Research Institution | Gifu University |
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Principal Investigator |
UENO Yoshihito Gifu University, Department of Biomolecular Science, Faculty of Engineering, Associate Professor, 工学部, 助教授 (20250467)
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| Project Period (FY) |
2004 – 2005
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| Project Status |
Completed (Fiscal Year 2005)
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| Budget Amount *help |
¥3,600,000 (Direct Cost: ¥3,600,000)
Fiscal Year 2005: ¥1,200,000 (Direct Cost: ¥1,200,000)
Fiscal Year 2004: ¥2,400,000 (Direct Cost: ¥2,400,000)
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| Keywords | nucleoside / nucleotide / DNA / triplex / protein / linker / antigene method / 核酸 / 三重鎖 / 3'-3'結合型 / 非対称 / 塩基三量体 / イノシン / キサントシン / ゲルシフト |
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| Research Abstract |
First, the synthesis and thermal stabilities of the triplexes containing either 2'-deoxyinosine (1) or 2'-deoxyxanthosine (3) in their second strands were examined. It was found that the triplexes with the 2'-deoxy-5-methylcytidine(dM)・1:dC and dM・1:dA base triplets are thermally stable, but those containing the dM・1:T and dM・1:dG base triplets are unstable under both neutral and slightly acidic conditions. On the other hand, it was found that the oligonucleotide containing 3 could form thermally stable triplexes with the oligonucleotides that involve four natural bases opposite the sites of 3. The rank of the thermal stabilities of the triplexes was as follows : the triplex containing the dM・3:dC base triplet > that containing the dM・3:dA base triplet > that containing the dM・3:T base triplet > that containing the dM・3:dG base triplet.
Furthermore, the synthesis of triplexes possessing an anthraquinonyl group and composed of branched oligonucleotides (ONs) was examined. Binding ability of a triplex-binding protein (MBP-LOR3^<ARF>) to the triplexes was evaluated by an electrophoretic mobility shift assay (EMSA). It was found that the triplex, which has an antraquinonecarbonyl group at the 5'-end of the third strand and is connected with the pentaerythritol linker, has greater affinity to the protein than an unmodified triplex.
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