Interaction of arylpiperazine ligands with the hydrophobic part of the 5-HT1A receptor binding site

Mario V Zlatović; Vladimir V Sukalović; Christoph Schneider; Goran M Roglić

doi:10.1016/j.bmc.2005.12.023

Interaction of arylpiperazine ligands with the hydrophobic part of the 5-HT1A receptor binding site

Bioorg Med Chem. 2006 May 1;14(9):2994-3001. doi: 10.1016/j.bmc.2005.12.023. Epub 2006 Jan 5.

Authors

Mario V Zlatović¹, Vladimir V Sukalović, Christoph Schneider, Goran M Roglić

Affiliation

¹ Faculty of Chemistry, University of Belgrade, PO Box 158, 11000 Belgrade, Serbia and Montenegro. mario@chem.bg.ac.yu

PMID: 16403641
DOI: 10.1016/j.bmc.2005.12.023

Abstract

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acids / chemistry
Binding Sites
Hydrophobic and Hydrophilic Interactions
Ligands
Models, Molecular
Piperazines / chemistry*
Piperazines / pharmacology*
Protein Structure, Tertiary
Receptor, Serotonin, 5-HT1A / chemistry*
Receptor, Serotonin, 5-HT1A / metabolism*
Static Electricity
Structure-Activity Relationship

Substances

Amino Acids
Ligands
Piperazines
Receptor, Serotonin, 5-HT1A