Development of methodology forchemical synthesis of proteins based on kinetically controlled peptide bond formation
| Project/Area Number |
23659055
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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 |
Drug development chemistry
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| Research Institution | The University of Tokushima |
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Principal Investigator |
OTAKA Akira 徳島大学, 大学院・ヘルスバイオサイエンス研究部, 教授 (20201973)
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| Project Period (FY) |
2011 – 2012
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| Project Status |
Completed (Fiscal Year 2012)
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| Budget Amount *help |
¥3,640,000 (Direct Cost: ¥2,800,000、Indirect Cost: ¥840,000)
Fiscal Year 2012: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2011: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
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| Keywords | ペプチド / チオエステル / 速度論的支配 / Native Chemical Ligation / タンパク質合成 / アシル転移 / 速度論的反応 / NCL / 速度論支配 / ペプチド合成 |
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| Research Abstract |
N-Sulfanylethylanilide (SEAlide) peptides were developed with the aim of achieving facile synthesis of peptide thioesters. The SEAlide moiety was proved to function as a thioester in the presence of phosphate salts and to participate in native chemical ligation (NCL) with N-terminal cysteinyl peptides, and this has served as a powerful protein synthesis methodology. The reactivity of a SEAlide peptide (anilide vs thioester) can be easily tuned with or without the use of phosphate salts. This interesting property of SEAlide peptides allows sequential three-fragment or unprecedented four-fragment ligation for efficient one-pot peptide/protein synthesis. Chemical synthesis of 162-residue GM2AP was achieved using the kinetically controlled ligation based on the SEAlide chemistry.
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Report
(3 results)
Research Products
(80 results)
