Acta Phys. -Chim. Sin. ›› 1998, Vol. 14 ›› Issue (10): 893-897.doi: 10.3866/PKU.WHXB19981007

• ARTICLE • Previous Articles     Next Articles

Structure-Affinity Relationship of lndole-Based for Phospholipase A2

Wang Ren-Xiao, Feng Ya-Bin, Lai Lu-Hua, Tang You-Qi   

  1. Institute of Physical Chemistry,Peking University,Beijing 100871
  • Received:1997-12-24 Revised:1998-04-20 Published:1998-10-15
  • Contact: Wang Ren-Xiao

Abstract:

 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.

Key words: Phospholipase A2, Indole-based inhibitors, Structure-based quantittive structure activity relationship, Drug design