2014 Fiscal Year Final Research Report
Analysis of prion protein aggregation mechanism by using that fragment peptides
| Project/Area Number |
24590066
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Physical pharmacy
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| Research Institution | Setsunan University |
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Principal Investigator |
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| Co-Investigator(Kenkyū-buntansha) |
KONISHI Motomi 摂南大学, 薬学部, 准教授 (20229446)
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| Project Period (FY) |
2012-04-01 – 2015-03-31
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| Keywords | プリオンタンパク質 / フラグメントペプチド / 酵素耐性 / 凝集性 / MT-MMP / カラムスイッチHPLC |
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| Outline of Final Research Achievements |
At first, we investigated the metal-binding ability of 21 synthetic peptides by column switch HPLC system composed of a metal chelate affinity column and an ODS reversed-phase column. Second, the conformational change by copper ion was analyzed by comparison of CD spectra. Third, each peptide was individually incubated with recombinant MT1-MMP, MT3-MMP, MMP-7 or human serum in the presence or absence of copper ion and the cleavage sites determined by LC-ESI-MS. The data obtained from this study suggest that MT-MMPs expressed in the brain might possess the degrading activity of prion protein. Finally, we analyzed the intermolecular interaction of hPrP fragment peptide by using a column switch HPLC system and AFFINIX QN system. The results obtained this experiment suggest that hPrP150-159 may play an important role for aggregation of hPrP.
We are now continuously investigating the key amino acid sequence for aggregation of hPrP and NMR analysis.
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| Free Research Field |
分析化学
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