| Project/Area Number |
12650861
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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 |
高分子合成
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| Research Institution | CHIBA UNIVERSITY |
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Principal Investigator |
YAMADA Norihiro CHIBA UNIVERSITY, FACULTY OF EDUCATION, ASSOCIATE PROFESSOR, 教育学部, 助教授 (40182547)
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| Project Period (FY) |
2000 – 2001
|
| Project Status |
Completed (Fiscal Year 2001)
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| Budget Amount *help |
¥3,700,000 (Direct Cost: ¥3,700,000)
Fiscal Year 2001: ¥700,000 (Direct Cost: ¥700,000)
Fiscal Year 2000: ¥3,000,000 (Direct Cost: ¥3,000,000)
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| Keywords | Alzheiraer's disease / β-sheet structure / hydrogen bonding / amyloid fibril / proline / peptide / amphiphile / organogel / FT-IR / リオトリピック液晶 |
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| Research Abstract |
Amphiphilic molecules that contain a tripeptide moiety form an aggregate not only in water but also in organic solvents. The aggregate possesses fibrous morphology and involves a rich amount of parallel β-sheet structure of peptides, which is similar to a β-peptide called an amyloid fibril. These similarities suggest that the tripeptide containing amphiphiles are suitable for an amyloid model. In the present study, we attempted to disintegrate the β-sheet assemblage by addition of a terminator molecule that lacked two proton donors for the interpeptide H-bonding. Aggregation of a tripeptide-containing amphiphile is accompanied by gel formation. The organogel turned into a light solution by addition of the terminator molecule.
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