THE CHEMICAL BIOLOGY OF NEW MICROBIAL ANTI-INFECTIVE AGENTS
Project/Area Number |
21310146
|
Research Category |
Grant-in-Aid for Scientific Research (B)
|
Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
Living organism molecular science
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Research Institution | Kitasato University |
Principal Investigator |
|
Co-Investigator(Renkei-kenkyūsha) |
INOKOSHI Junji 北里大学, 薬学部, 准教授 (30151640)
UCHIDA Ryuji 北里大学, 薬学部, 講師 (60280632)
KOYAMA Nobuhiro 北里大学, 薬学部, 助教 (60439156)
NAGAMITSU Toru 北里大学, 薬学部, 教授 (90300756)
UMEYAMA Hideaki 北里大学, 薬学部, 教授 (20050619)
|
Project Period (FY) |
2009 – 2011
|
Project Status |
Completed (Fiscal Year 2011)
|
Budget Amount *help |
¥17,290,000 (Direct Cost: ¥13,300,000、Indirect Cost: ¥3,990,000)
Fiscal Year 2011: ¥4,680,000 (Direct Cost: ¥3,600,000、Indirect Cost: ¥1,080,000)
Fiscal Year 2010: ¥4,680,000 (Direct Cost: ¥3,600,000、Indirect Cost: ¥1,080,000)
Fiscal Year 2009: ¥7,930,000 (Direct Cost: ¥6,100,000、Indirect Cost: ¥1,830,000)
|
Keywords | 感染症 / 天然物 / ケミカルバイオロジー / 標的分子 / 結合タンパク質 / ケミカルバイォロジー |
Research Abstract |
The mechanism of action of three anti-infective agents was studied. Lariatin A showed selective growth inhibition against mycobacteria. The proteins that bind to lariatin A were investigated in the lysate of Mycobacterium smegmatis, which led to the identification of MSMEG1878 protein whose function has not been reported. Cyslabdan potentiated ss-lactam imipenem activity against methicillin-resistant Staphylococcus aureus(MRSA). The proteins that bind to cyslabdan were investigated in the lysate of MRSA, which led to the identification of SAR1388, which is involved in the synthesis of the pentaglycine interpeptide bridge of the MRSA peptidoglycan. Furthermore, the docking model of viridicatumtoxin and UPP synthase was investigated in silico to elucidate the binding mode of spirohexalines.
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Report
(4 results)
Research Products
(64 results)