| Project/Area Number |
10650842
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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 |
Synthetic chemistry
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| Research Institution | The University of Tokyo |
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Principal Investigator |
YASHIRO Morio The Univ. Tokyo, Graduate School of Eng., Associate Professor, 大学院・工学系研究科, 助教授 (30192785)
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| Co-Investigator(Kenkyū-buntansha) |
KOMIYAMA Makoto The Univ. Tokyo, Graduate School of Eng., Professor, 大学院・工学系研究科, 教授 (50133096)
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| Project Period (FY) |
1998 – 1999
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| Project Status |
Completed (Fiscal Year 1999)
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| Budget Amount *help |
¥2,800,000 (Direct Cost: ¥2,800,000)
Fiscal Year 1999: ¥1,400,000 (Direct Cost: ¥1,400,000)
Fiscal Year 1998: ¥1,400,000 (Direct Cost: ¥1,400,000)
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| Keywords | peptide / amino acid / artificial peptidase / artificial hydras / multinuclear complex |
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| Research Abstract |
A novel catalysts for chemical modification and/or sequence-specific hydrolysis of peptides were studied.
(1) Condensation of glycine with various aldehydes yields β-hydroxyalkyl-substituted glycine, such as serine, threonine, or β-hydroxyphenylalanine. By this study, the followings have been found about this reaction, which open a new way to the chemical modification of peptides and proteins.
・ The condensations are remarkably accelerated by multinuclear cupper (II) complexes under mild conditions. The multinuclear complexes work as catalysts resulting a turnover more than unity for the first time.
・ An N-terminus glycine residue in oligopeptids is selectively converted into a serine residue by this reaction.
・ The trinuclear cupper (II) complex also catalyses oxidative decomposition of amino acids. The trinuclear complex is found to be useful for oxigenation of alkenes under mild conditions.
(2) Efficient and sequence-specific hydrolysis of peptides is found to be achieved by cooperation of a metal ion and an internal OH group in the side chain of a peptide. The generality of the specific scission is confirmed by tests using various tripeptides and tetrapeptides.
The presence of a histidine residue, which can coordinate metal ion that acts as a catalyst, near the serine residue remarkably enhances the efficiency of the hydrolysis.
An alkyl subsitution of the amino acid residue at the N-terminus site of the cleaved peptide bond enhances the rate for the metal-ion-catalysed hydrolysis.
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