Interaction of arylpiperazine ligands with the hydrophobic part of the 5-HT1A receptor binding site.
A flexible docking of a series of arylpiperazine derivatives with structurally different aryl part to the binding site of a model of human 5-HT1A receptor was exercised. The influence of structure and hydrophobic properties of aryl moiety on binding affinities was discussed and a model for ligand binding in the hydrophobic part of the binding site was proposed.
Zlatović
Mario V
MV
Faculty of Chemistry, University of Belgrade, PO Box 158, 11000 Belgrade, Serbia and Montenegro. mario@chem.bg.ac.yu
Sukalović
Vladimir V
VV
Schneider
Christoph
C
Roglić
Goran M
GM
D000596:Amino Acids / Q000737:chemistry; D001665:Binding Sites; D057927:Hydrophobic and Hydrophilic Interactions; D008024:Ligands; D008958:Models, Molecular; D010879:Piperazines / Q000737:chemistry* / Q000494:pharmacology*; D017434:Protein Structure, Tertiary; D044282:Receptor, Serotonin, 5-HT1A / Q000737:chemistry* / Q000378:metabolism*; D055672:Static Electricity; D013329:Structure-Activity Relationship
D000596:Amino Acids; D008024:Ligands; D010879:Piperazines; D044282:Receptor, Serotonin, 5-HT1A