| Project/Area Number |
07558130
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 試験 |
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| Research Field |
Biomedical engineering/Biological material science
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| Research Institution | Science University of Tokyo |
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Principal Investigator |
KATAOKA Kazunori Science University of Tokyo, Dept.of Materials Science, Professor, 基礎工学部, 教授 (00130245)
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| Project Period (FY) |
1995 – 1996
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| Project Status |
Completed (Fiscal Year 1996)
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| Budget Amount *help |
¥4,800,000 (Direct Cost: ¥4,800,000)
Fiscal Year 1996: ¥1,000,000 (Direct Cost: ¥1,000,000)
Fiscal Year 1995: ¥3,800,000 (Direct Cost: ¥3,800,000)
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| Keywords | peptide / polymeric micelle / poly (ethylene glycol) / poly (amino acid) / dynamic ligh scattering / polylysine / poly (aspartic acid) / pyrene / ブロック共重合体 / α-アミノ酸N-カルボン酸無水物 / フェニルアラニン / ヒドロ桂皮酸 / ポリマーミセル |
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| Research Abstract |
A variety of poly (ethylene glycol) (PEG) /polyamino acid block copolymers was synthesized by initiating the ring opening polymerization of alpha-amino acid N-carboxyanhydride (NCA) from primary amino group settled on the chain end of alpha-methoxy-omega-amino-poly (ethylene glycol). After the removal of protecting group, hydrophobic moieties were introduced into the side chain of poly (amino acid) segments of the block copolymer to control the hydrophilic/hydrophobic balance, allowing to form stable and monodispersive polymeric micelle. Micelles were prepared by solvent-substituting technique in the presence of peptide models to obtain peptide-loaded polymeric micelles. A fluorescent dye, pyrene, was used as a model compound for peptides. Dynamic light scattering measurements revealed a formation of micelles with relatively narrow distribution from block copolymers with considerably high substitution degree of side chain. These micelles had a very low critical micelle concentration (-30mg/l), indicating that they are thermodynamically stable. Of interest, in the case of block copolymers of PEG with poly (L-lysine) substituted with hydrocynnamic acid (HCA), secondary structure of poly (L-lysine) segments changed from random to beta-sheet upon micellization, indicating a close relationship between micelle formation and secondary structure of poly (amino acid) segments forming the core. Pyrene in the micelle was shown to be stably entrapped in the core, suggesting a promising feature of these micelles as novel peptide carriers.
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