title: Structure activity relationship studies of cinnamic acid derivatives as inhibitors of human neutrophil elastase revealed by ligand docking calculations.
abstract: Structure-activity relationship of cinnamic acid derivatives as inhibitors of the human neutrophil elastase is reported. Comparison of the inhibitory concentrations (IC50 values) with the results of the ligand docking calculations revealed that the structure element of the aromatic ortho-dihydroxy groups combined with a lipophilic residue seems to be a prerequisite for an optimal binding within the active site.
authors.affiliation: Institute of Pharmaceutical Biology, Albert-Ludwigs-University, Freiburg, Germany.
authors.forename: B
authors.initials: B
authors.lastname: Siedle
authors.forename: R
authors.initials: R
authors.lastname: Murillo
authors.forename: O
authors.initials: O
authors.lastname: Hucke
authors.forename: A
authors.initials: A
authors.lastname: Labahn
authors.forename: I
authors.initials: I
authors.lastname: Merfort
mesh_terms: D031885:Cimicifuga / Q000737:chemistry; D002934:Cinnamates / Q000138:chemical synthesis / Q000494:pharmacology*; D018360:Crystallography, X-Ray; D004791:Enzyme Inhibitors / Q000138:chemical synthesis / Q000494:pharmacology*; D006801:Humans; D007202:Indicators and Reagents; D019272:Leukocyte Elastase / Q000037:antagonists & inhibitors*; D008024:Ligands; D013329:Structure-Activity Relationship; D031208:Verbesina / Q000737:chemistry
chemical_list: D002934:Cinnamates; D004791:Enzyme Inhibitors; D007202:Indicators and Reagents; D008024:Ligands; D019272:Leukocyte Elastase