Pharmacophoric Search and 3D-QSAR Comparative Molecular Field Analysis Studies on Agonists of Melatonin Sheep Receptors

Journal of Medicinal Chemistry
1998.0

Abstract

Conformational analysis was used to characterize the agonist pharmacophore for melatonin sheep brain receptor recognition and activation. The molecular geometry shared by all conformations of the selected active ligands was determined. Assuming that all the compounds interact at the same binding site at the receptor level, 2-iodomelatonin pharmacophoric conformation served as a template for the superimposition of 64 structurally heterogeneous agonists constituting the training set used to perform a three-dimensional quantitative structure-activity relationship study via the comparative molecular field analysis method. A statistically significant model was obtained for the totality of the compounds (n = 64, q2 = 0.62, N = 6, r2 = 0.96, s = 0.28, F = 249) with steric, electrostatic, and lipophilic relative contributions of 28%, 35%, and 37%, respectively. The predictive power of the proposed model was discerned by successfully testing the 78 agonist ligands constituting the test set. The model so obtained and validated brings important structural insights to aid the design of novel melatoninergic agonist ligands prior to their synthesis.

Knowledge Graph

Similar Paper

Pharmacophoric Search and 3D-QSAR Comparative Molecular Field Analysis Studies on Agonists of Melatonin Sheep Receptors
Journal of Medicinal Chemistry 1998.0
Three-Dimensional Quantitative Structure−Activity Relationship of Melatonin Receptor Ligands:  A Comparative Molecular Field Analysis Study
Journal of Medicinal Chemistry 1997.0
Three-Dimensional Quantitative Structure−Activity Relationship Studies on Selected MT<sub>1</sub>and MT<sub>2</sub>Melatonin Receptor Ligands:  Requirements for Subtype Selectivity and Intrinsic Activity Modulation
Journal of Medicinal Chemistry 2003.0
Melatonin Receptor Ligands:  Synthesis of New Melatonin Derivatives and Comprehensive Comparative Molecular Field Analysis (CoMFA) Study
Journal of Medicinal Chemistry 1998.0
CoMFA-Based Prediction of Agonist Affinities at Recombinant D1 vs D2 Dopamine Receptors
Journal of Medicinal Chemistry 1998.0
Cytisine derivatives as high affinity nAChR ligands: synthesis and comparative molecular field analysis
Il Farmaco 2002.0
Design, Synthesis, and Evaluation of Novel A<sub>2A</sub> Adenosine Receptor Agonists
Journal of Medicinal Chemistry 2001.0
Conformationally Restrained Melatonin Analogues:  Synthesis, Binding Affinity for the Melatonin Receptor, Evaluation of the Biological Activity, and Molecular Modeling Study
Journal of Medicinal Chemistry 1997.0
Cytisine derivatives as high affinity nAChR ligands: synthesis and comparative molecular field analysis
Il Farmaco 2002.0
Comparative Molecular Field Analysis-Based Prediction of Drug Affinities at Recombinant D1A Dopamine Receptors
Journal of Medicinal Chemistry 1996.0