Structural elucidation of molecular basis of cytostatic activity of a novel peptide from a wild silkworm and its application
Project/Area Number |
24710240
|
Research Category |
Grant-in-Aid for Young Scientists (B)
|
Allocation Type | Multi-year Fund |
Research Field |
Living organism molecular science
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Research Institution | Hokkaido University |
Principal Investigator |
KAMIYA Masakatsu 北海道大学, 先端生命科学研究科(研究院), 助教 (30399810)
|
Project Period (FY) |
2012-04-01 – 2014-03-31
|
Project Status |
Completed (Fiscal Year 2013)
|
Budget Amount *help |
¥4,680,000 (Direct Cost: ¥3,600,000、Indirect Cost: ¥1,080,000)
Fiscal Year 2013: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2012: ¥3,510,000 (Direct Cost: ¥2,700,000、Indirect Cost: ¥810,000)
|
Keywords | 細胞増殖抑制活性 / ペプチド / 昆虫 / NMR / 機能性ペプチド / 相互作用解析 |
Research Abstract |
Yamamarin, a novel insect pentapeptide with an amidated C-terminus, has been isolated from diapausing pharate first-instar larvae of the wild silkmoth and is thought to be responsible for the regulation of diapause. Recently, this peptide significantly suppresses the proliferation of rat hepatoma (liver cancer) cells. This finding strongly suggests that yamamarin and its derivatives are promising candidates for use as therapeutic agents. However, its action mechanisms remain unknown. In this study, we investigated the interaction between yamamarin and fibrillarin. The following results were obtained. (1) We have successfully obtained a recombinant fibrillarin using E. coli expression system. (2) The CD results indicated that a recombinant fibrillarin was correctly folded. (3) The docking calculation suggested that yamamarin can bind to a substrate-binding site of fibrillarin.
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Report
(3 results)
Research Products
(21 results)
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[Journal Article] Interaction between tachyplesin I, an antimicrobial peptide derived from horseshoe crab, and lipopolysaccharide2014
Author(s)
Takahiro Kushibiki, Masakatsu Kamiya, Tomoyasu Aizawa, Yasuhiro Kumaki, Takashi Kikukawa, Mineyuki Mizuguchi, Makoto Demura, Shun-ichiro Kawabata, Keiichi Kawano
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Journal Title
Biochimica et Biophysica Acta - Proteins and Proteomics
Volume: 1,844
Issue: 3
Pages: 527-534
DOI
Related Report
Peer Reviewed
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[Journal Article] Role of Thr218 in the Light-Driven Anion Pump Halorhodopsin from Natronomonas pharaonis2013
Author(s)
Shibasaki, K., Shigemura, H., Kikukawa, T., Kamiya, M., Aizawa, T., Kawano, K., Kamo, N., Demura, M
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Journal Title
Biochemistry
Volume: 52
Issue: 51
Pages: 9257-9268
DOI
Related Report
Peer Reviewed
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[Journal Article] Synthesis and Characterization of Water-Soluble Silk Peptides and Recombinant Silk Protein Containing Polyalanine, the Integrin Binding Site, and Two Glutamic Acids at Each Terminal Site as a Possible Candidate for Use in Bone Repair Materials2013
Author(s)
Asakura, T., Suzuki, Y., Nagano, A., Knight, D.P., Kamiya, M., Demura, M.
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Journal Title
Biomacromolecules
Volume: 14
Issue: 10
Pages: 3731-3741
DOI
Related Report
Peer Reviewed
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[Journal Article] Overexpression of an antimicrobial peptide derived from C. elegans using an aggregation-prone protein coexpression system.2013
Author(s)
Tomisawa S, Hojo E, Umetsu Y, Ohki S, Kato Y, Miyazawa M, Mizuguchi M, Kamiya M, Kumaki Y, Kikukawa T, Kawano K, Demura M, Aizawa T
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Journal Title
AMB Express
Volume: 3
Issue: 1
Pages: 45-52
DOI
Related Report
Peer Reviewed
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