Self-assembly and the redox catalysis of porphyrins bearing β-sheet polypeptides
| Project/Area Number |
15550149
|
|---|
| Research Category |
Grant-in-Aid for Scientific Research (C)
|
| Allocation Type | Single-year Grants |
|---|
| Section | 一般 |
|---|
| Research Field |
Chemistry related to living body
|
|---|
| Research Institution | Kyushu Institute of Technology |
|---|
Principal Investigator |
ARAI Toru Kyushu Institute of Technology, Faculty of Engineering, Associate Professor, 工学部, 助教授 (50222716)
|
|---|
| Project Period (FY) |
2003 – 2004
|
| Project Status |
Completed (Fiscal Year 2004)
|
| Budget Amount *help |
¥3,900,000 (Direct Cost: ¥3,900,000)
Fiscal Year 2004: ¥800,000 (Direct Cost: ¥800,000)
Fiscal Year 2003: ¥3,100,000 (Direct Cost: ¥3,100,000)
|
|---|
| Keywords | porphyrin / polypeptide / self-assembly / beta-sheet structure / redox / hemeenzyme / catalytic reaction / CD spectrum |
|---|
| Research Abstract |
1.Self-assembly of porphyrins bearing β-sheet peptides : Two porphyrin-porphyrin interactions were observed for the self-assembled porphyrins linking pentapeptides, whereas the interaction between the neighboring porphyrins was weakened for the porphyrins linking heptapeptide. NMR measurement showed the stacking of the porphyrin moieties.
2.Interaction between metalloporphyrins tethered to a β-sheet peptide : NMR measurement showed edge-to-edge orientations between Zinc and Cobalt (III) porphyrins assembled on a natural β-sheet peptide. The face-to-face interaction was observed only when the bridging ligand, 4.4'-dipyridyl, was added.
3.Peroxidase activity of a βαβα-peptide bearing the iron porphyrin : Iron porphyrin was covalently linked to a 49-mer peptide with the βαβα-structure. The peroxidase activity using cumene hydroperoxide as the oxidant was analyzed and the assembling of the multiple porphyrins was suggested.
|
Report
(3 results)
Research Products
(12 results)
