Synthesis of partial structure of glycolipid MPIase for elucidating the mechanism on membrane protein integration in the inner membrane of E. coli.

2016 Fiscal Year Final Research Report

• 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
• Keywords: 糖脂質 / 膜タンパク質 / 膜挿入

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.

Free Research Field

糖鎖合成化学