ISSN 1000-6818CN 11-1892/O6CODEN WHXUEU
Acta Phys Chim Sin >> 1998,Vol.14>> Issue(10)>> 893-897     doi: 10.3866/PKU.WHXB19981007         中文摘要
Structure-Affinity Relationship of lndole-Based for Phospholipase A2
Wang Ren-Xiao, Feng Ya-Bin, Lai Lu-Hua, Tang You-Qi
Institute of Physical Chemistry,Peking University,Beijing 100871
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 A new method which can estimate the binding affinity of an enzyme-ligand complex was applied to studying the indole-based inhibitors for human synovial fluid phospholipase A2.The three-dimensional structures of phospholipase-inhibitor complexes were modeled by molecular docking and energy minimization. The bindmg affinities were calculated by program SCORE. All together 12 inhibitors were analyzed .The calc The calculated IC50 values fit well with the experimentally observed values By contrast, CoMFA studies of the same series of inhibitors yielded much poorer results. From SCORE's output, the pharmacophorc of phospholipase A2 inhibitors was also derived, which is valuable for designing novel inhibitors.

Keywords: Phospholipase A2   Indole-based inhibitors   Structure-based quantittive structure activity relationship   Drug design  
Received: 1997-12-24 Accepted: 1998-04-20 Publication Date (Web): 1998-10-15
Corresponding Authors: Wang Ren-Xiao Email:

Cite this article: Wang Ren-Xiao, Feng Ya-Bin, Lai Lu-Hua, Tang You-Qi. Structure-Affinity Relationship of lndole-Based for Phospholipase A2[J]. Acta Phys. -Chim. Sin., 1998,14 (10): 893-897.    doi: 10.3866/PKU.WHXB19981007
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