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 bi...

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Bibliographic Details
Published in:Bioorganic & medicinal chemistry 2006-05, Vol.14 (9), p.2994-3001
Main Authors: ZLATOVIE, Mario V, SUKALOVIE, Vladimir V, SCHNEIDER, Christoph, ROGLIE, Goran M
Format: Article
Language:English
Subjects:
Amino Acids - chemistry
Binding Sites
Biological and medical sciences
Hydrophobic and Hydrophilic Interactions
Ligands
Medical sciences
Models, Molecular
Neuropharmacology
Neurotransmitters. Neurotransmission. Receptors
Pharmacology. Drug treatments
Piperazines - chemistry
Piperazines - pharmacology
Protein Structure, Tertiary
Receptor, Serotonin, 5-HT1A - chemistry
Receptor, Serotonin, 5-HT1A - metabolism
Serotoninergic system
Static Electricity
Structure-Activity Relationship
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Summary: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.
ISSN:0968-0896
1464-3391
DOI:10.1016/j.bmc.2005.12.023