2001 Fiscal Year Final Research Report Summary
Study on molecular architecture and its application
| Project/Area Number |
10145102
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| Research Category |
Grant-in-Aid for Scientific Research on Priority Areas (A)
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| Allocation Type | Single-year Grants |
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| Research Institution | Tokyo University of Agriculture and Technology |
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Principal Investigator |
MATSUNAGA Tadashi Faculty of Technology, Tokyo University of Agriculture and Technology, Professor, 工学部, 教授 (10134834)
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| Co-Investigator(Kenkyū-buntansha) |
GOTO Masahiro Graduate School of Engineering, Kyushu University, Associate Professor, 大学院・工学研究院, 助教授 (10211921)
KOMIYAMA Makoto Graduate School of Engineering, The University of Tokyo, Professor, 先端科学技術研究センター, 教授 (50133096)
KOBATAKE Eiry Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, Associate Professor, 大学院・生命理工学研究科, 助教授 (00225484)
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| Project Period (FY) |
1998 – 2001
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| Keywords | Molecular archtecture / Bacterial magnetic particles / Protein A / Lipid-tagged antibody / lipospme / β-Cyclodextrin / Surfactant / Synthesized sugar lipid |
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| Research Abstract |
In cell surface, many recepter proteins are presented and the specific biomolecules are recognized by these recepter proteins. These mechanisms can be analyzed from chemical view points. To systemize the biotergeting, the molecular architecture of these biomolecules were investigated. Dr. Matsunaga studied molecular architecture using bacterial magnetic particles (BMPs). Successful display of functional proteins such as luciferase, proteinA and receptor on BMP was demonstrated using anchor proteins, MagA or a newly isolated BMP membrane protein Mms16, through gene fusion. ProteinA-displayed BMPs was used for chemiluminescence immunoassay of insulin and high sensitive assay. Furthermore, expression of active receptor on BMPs for estrogen binding assay was also confirmed. A novel approach, in vitro direct insertion, for immobilizing functional proteins on BMPs using the native protein, MagA was developed. Through this technique, active luciferase could be successfully displayed on BMPs.
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Dr. Kobatake studied the displaying method using site-specific lipid-tagged anti-2-phenyl -oxazolone single-chain antibody and lipid-tagged antibody-binding protein were prepared by genetic engineering for displaying antibody molecules on liposome surfaces. The lipid-tagged proteins were expressed in E. coli and translocated at the bacterial membrane. They were stably incorporated into liposomes with high orientation by anchoring the lipid-tail into the hydrophobia layer on the liposome membrane. Dr. Komiyama studied the cross-linkage of β-cyclodextrin (β-CyD) with diisocyante linker and molecular imprinting to the molecule. It was suggested that the molecular imprinting effect is effective in regulating host molecules to cooperatively bind guest molecules. Dr.Goto studied the architecture on the liposome surface. The reaction rate of the surfactant-protease complex was 100 times higher than that of the native one. A biotargeting effect of liposomes that includes the newly synthesized sugar lipid was studied. The degree of targeting effect of liposome was evaluated by the binding test and it was found that the sugar lipid exhibited an excellent bio-targeting effect. Less
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Research Products
(12 results)
