高等学校化学学报 ›› 1998, Vol. 19 ›› Issue (S1): 200.

• Organic Synthesis Chemistry • 上一篇    下一篇

Design,Synthesis and Activities of Cyanouracils Photosystem Ⅱ Inhibitors Basen on D1 Protein

Huayin Liu, Huifen Tan, Huazheng Yang   

  1. Institute of Elemento-Organic Chemistry, National Key Laboratory of Elemento-Organic Chemistry Nankai University, Tianjin 300071
  • 出版日期:1998-12-31 发布日期:1998-12-31
  • 基金资助:
    This study was supported by grants from the Youth Science Fundation of China (No: 29702006)

Design,Synthesis and Activities of Cyanouracils Photosystem Ⅱ Inhibitors Basen on D1 Protein

Huayin Liu, Huifen Tan, Huazheng Yang   

  1. Institute of Elemento-Organic Chemistry, National Key Laboratory of Elemento-Organic Chemistry Nankai University, Tianjin 300071
  • Online:1998-12-31 Published:1998-12-31
  • Supported by:
    This study was supported by grants from the Youth Science Fundation of China (No: 29702006)

摘要: The study on the interaction between protein target and little molecules can help design new drugs, which have more selective and higher activities. A large number of inhibitors,including ureas, triazines and phenols etc.,are known to block photosystem Ⅱ by displacing plastoquinone from the QB-binding niche of the D1 protein in the reaction center. The X-ray crystall structure of D1 protein in high plant is unknown, but the X-ray crystal structure of L protein of photosynthetic reaction centre of Rps. Viridis has already proved in 80'. Based on this structure, the 3D-structure of Pisnm Saihmm 32Kdal (Dl) was constructed by homology modeling method, and the properties, such as steric, hydrophobic, electrostatic properties of active sites region of the Dl protein were also characterized by Grid Search method with probes of CH3E, H2O, NT and proton.The detail proposal of the model will be shown elsewhere.

Abstract: The study on the interaction between protein target and little molecules can help design new drugs, which have more selective and higher activities. A large number of inhibitors,including ureas, triazines and phenols etc.,are known to block photosystem Ⅱ by displacing plastoquinone from the QB-binding niche of the D1 protein in the reaction center. The X-ray crystall structure of D1 protein in high plant is unknown, but the X-ray crystal structure of L protein of photosynthetic reaction centre of Rps. Viridis has already proved in 80'. Based on this structure, the 3D-structure of Pisnm Saihmm 32Kdal (Dl) was constructed by homology modeling method, and the properties, such as steric, hydrophobic, electrostatic properties of active sites region of the Dl protein were also characterized by Grid Search method with probes of CH3E, H2O, NT and proton.The detail proposal of the model will be shown elsewhere.

TrendMD: