| Budget Amount *help |
¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000)
Fiscal Year 2009: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2008: ¥3,120,000 (Direct Cost: ¥2,400,000、Indirect Cost: ¥720,000)
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| Research Abstract |
Glycopeptide mucins and IgA1 hinge region PSTPPTPSPSTPPTPSPS found in human were synthesized under microwave irradiation atmosphere and the three-dimensional structure analysis was performed.
In the case of IgA1 hinge, the glycopeptides with N-acetylgalactosamine (GalNAc) and core1 structure (Gal - GalNAc) were synthesized in the residue indicated by underlines.
As a result, 9 of proline formed an isomer of cis - trans out of a peptide without sugar, but a isomerizaton of cis - trans was drastically restrained to add a sugar chain modification (in particular, in the case of core1 structure), and that a structure with trans conformation exists mainly became clear. It was revealed that glycans on serine or threonine restrains an isomerizaton reaction of the proline which exists in the C-terminal side.
General solid phase synthesis of peptide is initiated from the C-termininal, but it is widely known that the yield decrease in the case of the first amino acid is proline because the peptide structure constructs a ring structure (diketopiperazin structure) in a deprotection reaction after the coupling. This is because proline forms a cis conformer, the knowledge obtained by IgA1 research, when I substitute for the 2nd amino acid in a sugar amino acid, proline is fixed on a trans conformer, and amino acid extension has occurred. A PCT application was performed about the case that a sugar chain has the effect which maintains the proline which exists next to the C-terminal as a trans conformer (cis-trans isomerizaton reaction slowed down.) and a Fmoc solid phase peptide synthesis method in the case of proline possesses in the C-terminal as a result of this research.
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