| Budget Amount *help |
¥3,700,000 (Direct Cost: ¥3,700,000)
Fiscal Year 2005: ¥1,800,000 (Direct Cost: ¥1,800,000)
Fiscal Year 2004: ¥1,900,000 (Direct Cost: ¥1,900,000)
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| Research Abstract |
The irreversible protein denaturation due to the aggregation is serious problem in the research of protein structure. Molecular chaperones, member of heat shock protein, prevent the protein aggregate in vivo through the weak protein integration. It has been shown that phospholipid polymers (MPC polymer) also weakly interact proteins, and we used these polymers as the artificial molecular chaperone. We have design several MPC copolymers, and screened by there chaperone-like activity. The activity for the refolding of β-galactosidase, malate dehydrogenase, MHC Class II, luciferase GFP and rhodanese have been examined. The copolymer with butylmethacrylate (PMB polymer) showed high performance for the refolding of these proteins.
The in vitro protein synthesis is one of the effective methods for this purpose, but this method has weak point of the low yield. To construct a highly efficient in vitro protein synthesis system, the effects PMB polymer were examined. Although PMB polymer showed chaperone-like activity, the yield of rhodanese in the in vitro protein synthesis was not enhanced by this polymers. Another new design of the MPC polymer is necessary for the efficient in vitro protein synthesis system. Furthermore, we examined the effect of MPC copolymers on the amyloid fibril formation of insulin. We found that hydrophilic copolymers accelerated the amyloid formation rate, and the hydrophobic copolymers reduced the total amount of amyloid fibril. But so far, MPC copolymers don't have sufficient ability to control amyloid fibril structure. We will improve the functional capability of MPC copolymer by the arrangement of copolymerization ratio and molecular weight.
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