title: Comparative amino acid decomposition analysis of potent type I p38α inhibitors.
abstract: OBJECTIVE
  p38α is a member of mitogen-activated protein kinases (MAPK) considered as a prominent target in development of anti-inflammatory agents. Any abnormality in the phosphorylation process leads to the different human diseases such as cancer, diabetes and inflammatory diseases. Several small molecule p38α inhibitors have been developed up to now. In this regard, structural elucidation of p38 inhibitors needs to be done enabling us in rational lead development strategies.
  
  
  METHODS
  Various interactions of three potent inhibitors with p38α active site have been evaluated in terms of binding energies and bond lengths via density function theory and MD simulations.
  
  
  RESULTS
  Our comparative study showed that both ab initio and MD simulation led to the relatively similar results in pharmacophore discrimination of p38α inhibitors.
  
  
  CONCLUSIONS
  The results of the present study may find their usefulness in pharmacophore based modification of p38α inhibitors.
authors.affiliation: Medicinal and Natural Products Chemistry Research Center, Shiraz University of Medical Sciences, PO Box 3288-71345, Shiraz, Iran. mirir@sums.ac.ir.
authors.forename: Ahmad
authors.initials: A
authors.lastname: Ebadi
authors.forename: Nima
authors.initials: N
authors.lastname: Razzaghi-Asl
authors.forename: Mehdi
authors.initials: M
authors.lastname: Khoshneviszadeh
authors.forename: Ramin
authors.initials: R
authors.lastname: Miri