| Budget Amount *help |
¥2,730,000 (Direct Cost: ¥2,100,000、Indirect Cost: ¥630,000)
Fiscal Year 2013: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2012: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
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| Research Abstract |
Pr55Gag of human immunodeficiency virus, the principal structural component required for virus assembly, is known to bind D-myo-phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2). The N-terminus of Pr55Gag, MA domain, plays a critical role in the binding of Pr55Gag to the plasma membrane. We designed and synthesized PI(2,3,4,5,6)P5 analogs comprising highly phosphorylated inositol and variously modified diacylglycerol to examine the MA-binding property. The binding affinity for MA of Di-C7-PI(2,3,4,5,6)P5 (compound 2) is 70-fold higher than that of PI(4,5)P2 having the similar carbon length, suggesting the possibility of the PIP5 analog to block the Pr55Gag membrane binding by competing with PI(4,5)P2 in the MA-binding.
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