2002 Fiscal Year Final Research Report Summary
Development of glyco-cluster materials systems to detect and neutralize pathogenic microorganisms
| Project/Area Number |
13558108
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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 | 展開研究 |
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| Research Field |
Biomedical engineering/Biological material science
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| Research Institution | Nagoya University |
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Principal Investigator |
KOBAYASHI Kazukiyo Nagoya University, Department of Molecular Design & Engineering, Graduate School of Engineering, Professor, PhD, 工学研究科, 教授 (10023483)
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| Co-Investigator(Kenkyū-buntansha) |
MIURA Yoshiko Nagoya University, Department of Molecular Design & Engineering, Graduate School of Engineering, Assistant Professor, PhD., 工学研究科, 助手 (00335069)
NISHIDA Yoshihiro Nagoya University, Department of Molecular Design & Engineering, Graduate School of Engineering, Associate Professor, PhD, 工学研究科, 助教授 (80183896)
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| Project Period (FY) |
2001 – 2002
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| Keywords | carbohydrates / biomaterials / polymers / molecular recognition / influenza virus / vero toxins / ruthenium complexes |
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| Research Abstract |
Influenza viruses and pathogenic E.coli species are epidemic and sometimes critical for infants and aged patients. These pathogens invade our bodies through cell surface oligosaccharides. Sialo oligoaccharides and α(l-4)-galactobiosyl oligosaccharides on cell surfaces are the recovnition signals respectively for influenza viruses and E.coli Shiga toxins (Stx-I and Stx-II). The present research is aimed at developing polymer-based biomaterials having multivalent sialo and α(l-4)-Gal arrays to detect, capture, and neutralize influenza-viruses and vero toxins.
We have succeeded in one-pot transglycosylation of disialo complex-type oligosaccharides onto an α-glucose-functionalized tris-bipyridine ruthenium complex. The resulting glycoconjugates exhibited excellent lectin-affinities comparable to that of polymers presenting multiple sialoside arrays. Also, they have strong luminescence that is markedly depressed by addition of virus, probably due to disruption of their saccharide-shell structures.
We have found the potential utility of the galacto-trehalose α(l-l)-linkage as a promising substitute for the globosyl α(l-4)-linkage. Though the binding of the galacto-trehalose to Stx-I and Stx-II, particularly to the latter, is still weaker than that of the natural Gb_2 and Gb_3 globosides, galacto-trehalose may integrate the binding affinity significantly by additionally introducing β-glucoside moiety or related other units.
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