2001 Fiscal Year Final Research Report Summary
DEVELOPMENT OF THERAPUETIC AGENTS AGAINST VERO TOXIN PRODUCED BY E. COLI
| Project/Area Number |
11557197
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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 |
医薬分子機能学
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| Research Institution | Kinki University |
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Principal Investigator |
FUJII Masayuki KINKI UNIVERSSITY, KYUSHU SCHOOL OF ENGINEERING, PROFESSOR, 九州工学部, 教授 (60199297)
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| Project Period (FY) |
1999 – 2001
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| Keywords | Vero toxin / Gb3 ceramide / 28SrRNA / inhibitors |
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| Research Abstract |
Synthesis and characterization of specific inhibitor and detection probe of vero toxin (VT) produced by enterobacterium O-157 were studied. Molecular design based on detail analysis of reaction mechanisms of N-glycosidase activity of vero toxin was performed. Analogous molecules of 28S rRNA which is a substrate for vero toxin A chain and globotriose (Gb3) ceramide which is a glycoreceptor on cell surface for vero toxin B chain. Inhibitory effects of some analogous RNA molecules which have GAGA tetraloop structure in common were evaluated by conventional experiments and showed that 2'-OMe anaolgs and phosphorothioate analogs were promising structure for drug application because those structures are known to be stable in physiological conditions in cells and even in vivo. Gb3 analogs bearing biotin moiety were prepared and immobilized on SPR sensor tip. Obsevations of binding affnities of the Gb3 analogs and abrin C which has the same specificity of sugar binding as vero toxin suggested that synthesized analogs were good detection probes for vero toxin. Fluorecein labeled Gb3 analogs and some other sugar derivatives were revealed that they are also good probes for the detection of VT using a fluorospectrometer.
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[Publications] Takanori Kubo, Kinuko Yokoyama, Ryoji Ueki, Shinya Abe, Koichiro Goto, Takuro Niidome, Haruhiko Aovagi, Kaoru Iwakuma, Setsuko Ando, Shin Ono and Masayuki Fujii: "Design, Synthesis and Characterization of DNA Binding Peptides"Peptide Science. 2000. 109-112 (2001)
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