| Project/Area Number |
16550142
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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 |
Chemistry related to living body
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| Research Institution | Nagoya Institute of Technology |
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Principal Investigator |
INAI Yoshihito Nagoya Institute of Technology, Graduate School of Engineering, associate professor, 大学院・工学研究科, 助教授 (60223210)
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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 |
¥2,400,000 (Direct Cost: ¥2,400,000)
Fiscal Year 2005: ¥1,000,000 (Direct Cost: ¥1,000,000)
Fiscal Year 2004: ¥1,400,000 (Direct Cost: ¥1,400,000)
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| Keywords | chirality / peptide / helical structure / dehydroamino acid / circular dichroism / computational chemistry / chiral induction / helix sense |
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| Research Abstract |
This project aims to clarify chirality transfer route and chirality amplification inherent in protein backbone. To focus on these issues, optically-inactive helical backbones of peptides have been mainly used. In particular, we have investigated chirality transfer to peptide helix in peptide chain-chiral moiety, peptide-peptide chains, and peptide aggregates. The following points have been mainly achieved.
・A mechanism for intermolecular interaction and chiral complex formation on the N-terminus of peptide helix has been confirmed.
・Chirality induction in peptide chain or chirality transfer along a helical chain have been observed for several peptide sequences.
・Influences of external condition and stimulus on peptide chirality have been demonstrated for sequences that incorporating. chiral residue(s) into specific positions of optically-inactive segments.
・CD spectra and transition states of peptides containing dehydroresidues have been predicted from molecular orbital calculations.
・Information on chemical structure-chirality induction has been obtained in chiral interactions between helical chains.
・Information about oligopeptide aggregation and chirality amplification has been obtained.
・Influence of internal chirality and solvent effect on CD signals of peptide linked by two chains has been preliminary studied.
・Chiral interactions in solid state and aqueous solution as peptide aggregates have been investigated to offer us further direction to our research.
Apart of these findings and achievements has been summarized on the following academic journals.
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