| Project/Area Number |
18550103
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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 |
Polymer chemistry
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| Research Institution | Akita University |
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Principal Investigator |
JIKEI Mitsutoshi Akita University, Department of Engineering in Applied Chemistry, Professor (70251618)
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| Co-Investigator(Kenkyū-buntansha) |
ITOH Hideaki Akita University, Department of Engineering in Applied Chemistry, Professor (80168369)
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| Project Period (FY) |
2006 – 2007
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| Project Status |
Completed (Fiscal Year 2007)
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| Budget Amount *help |
¥4,220,000 (Direct Cost: ¥3,800,000、Indirect Cost: ¥420,000)
Fiscal Year 2007: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2006: ¥2,400,000 (Direct Cost: ¥2,400,000)
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| Keywords | Nano Materials / Enzymatic Degradation / Biomaterial / Dendrimer / 酵素 |
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| Research Abstract |
Lysine Dendrimers prepared from L-lysine as a starting material are expected to be biocompatible and biodegradable nano materials for biomedical applications, such as drug delivery and gene therapy. The branching architecture is usually prepared by the coupling reaction of both α-and ε-amino groups with the carboxylic group of lysine. Since the ε-amino group plays important roles in biological recognition, the luck of ε-amino group reduces the degradability of the lysine dendrimers by enzymes. The reduced degradability may cause the accumulation of the lysine dendrimer when injected to a living body. The research project aims to produce new enzyme-degradable dendrimers for biomedical application. In order to achieve the goal, a series of lysine dendrimers which remain the ε-amino group of each lysine was prepared. The study on the degradation of the novel lysine dendrimers by enzymes was also planned to evaluate the effect of the ε-amino group on enzymatic degradation.
The trimer and te
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tramer composed of glycine and lysine were designed as building blocks for the novel lysine dendrimers. The peptide oligomers were prepared by conventional solid-phase synthesis on the acid sensitive trityl-resin. The α-and ε-amino groups of the peptide oligomers were protected by 9-fluorenylmethoxycarbonyl (Fmoc) and t-butoxycarbonyl (BOC) groups, respectively. The structure of the peptide oligomers was confirmed by NMR and MALDI-TOF MS spectroscopic measurements. The lysine dendrimers were prepared using the peptide oligomers as building blocks by Fmoc solid-phase synthetic strategy on Wang-resin. The final cleavage by trifluoroacetic acid resulted in the formation of the deprotected lysine dendrimers which had the ε-amino groups on each building unit. The each generation one and two dendrimer purified by preparative HPLC showed a single peak by analytical HPLC. The molecular weight of the dendrimers was confirmed by the MALDI-TOF MS measurement. It was also observed that the cleavage of the BOC groups required prolonged reaction time in comparison with the case of deprotection of BOC groups for conventional peptide syntheses. The preparation of high-generation dendrimers from the peptide oligomers and the enzymatic degradation study have been postponed due to the difficulty in mass production of the peptide oligomer. Although the term of this research project supported by Grand-in-Aid for scientific research c was finished, the project has continuously been pursued in order to create new enzyme-degradable dendrimers. Less
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