Synthesis of partial structure of glycolipid MPIase for elucidating the mechanism on membrane protein integration in the inner membrane of E. coli.
| Project/Area Number |
15H06844
|
|---|
| Research Category |
Grant-in-Aid for Research Activity Start-up
|
| Allocation Type | Single-year Grants |
|---|
| Research Field |
Biomolecular chemistry
|
|---|
| Research Institution | Suntory Foundation for Life Sciences |
|---|
Principal Investigator |
FUJIKAWA Kohki 公益財団法人サントリー生命科学財団, 生物有機科学研究所・構造生命科学研究部, 研究員 (50755874)
|
|---|
| Project Period (FY) |
2015-08-28 – 2017-03-31
|
| Project Status |
Completed (Fiscal Year 2016)
|
| Budget Amount *help |
¥2,730,000 (Direct Cost: ¥2,100,000、Indirect Cost: ¥630,000)
Fiscal Year 2016: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2015: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
|
|---|
| Keywords | 糖脂質 / 膜タンパク質 / 膜挿入 / 有機化学 / 生体分子 / 有機合成化学 |
|---|
| Outline of Final Research Achievements |
Trisaccharide of MPIase, which can elongate saccharide unit and can introduce Ac group into 6-OH of GlcNAc was synthesized from properly designed monosaccharide unit. Trisaccharide obtained was phosphorylated and was coupled with phosphatidic acid for the synthesis of minimum structure of MPIase, named as mini-MPIase. Both mini-MPIase with Ac group and mini-MPIase without Ac group were subjected into membrane protein integration test. Mini-MPIase with Ac group showed 25% integration ability of natural MPIase, while mini-MPIase without Ac group provided almost no integration ability. These results indicate that some extent length of the saccharide and 6-OAc group of GlcNAc are critical for the membrane protein integration in the inner membrane of E. coli.
|
Report
(3 results)
Research Products
(4 results)
