Library design and selection for obtaining peptides that target HTLV-1 protein
| Project/Area Number |
25560401
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| Research Category |
Grant-in-Aid for Challenging Exploratory Research
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| Allocation Type | Multi-year Fund |
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| Research Field |
Biomolecular chemistry
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| Research Institution | Kyoto University |
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Principal Investigator |
FUTAKI Shiroh 京都大学, 化学研究所, 教授 (50199402)
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| Co-Investigator(Renkei-kenkyūsha) |
MATSUOKA Masao 京都大学, ウイルス研究所, 教授 (10244138)
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| Project Period (FY) |
2013-04-01 – 2015-03-31
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| Project Status |
Completed (Fiscal Year 2014)
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| Budget Amount *help |
¥3,900,000 (Direct Cost: ¥3,000,000、Indirect Cost: ¥900,000)
Fiscal Year 2014: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2013: ¥2,340,000 (Direct Cost: ¥1,800,000、Indirect Cost: ¥540,000)
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| Keywords | 成人T細胞白血病 / ヒトT細胞白血病ウイルス / HTIL-1 HBZ / コイルドコイル / Hitchhiker法 / ヒトT細胞白血病ウイルスI型 / HTLV-1 HBZ / HTLV-I HBZ |
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| Outline of Final Research Achievements |
The genome of HTLV-1 encodes the basic leucine zipper protein, HTLV-1 bZIP factor (HBZ). HBZ has a domain containing a cFos-like leucine-zipper segment, which confers interaction of HBZ to cJun and related protein. Peptides that specifically block the interaction of HBZ with Jun related proteins could be powerful tools in order to elucidate the role of the interaction in the onset of ATL. By focusing on the a-g interaction, successful design and selection were accomplished to obtain a leucine-zipper segment that discriminates the appropriate partner over another that provides very similar patterns of electrostatic interactions. Employing the Hitchhiker Translocation in vivo selection system, we have succeeded in acquiring a mutated cJun-derived leucine-zipper segment that shows significantly higher affinity towards leucine-zipper of HBZ than that of cFos.
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Report
(3 results)
Research Products
(2 results)
