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G Protein-coupled Receptors01:15

G Protein-coupled Receptors

G Protein-Coupled Receptors or GPCRs are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to sensory stimuli such as light, odors, hormones, cytokines, or neurotransmitters.
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Structure-Activity Relationships and Drug Design01:28

Structure-Activity Relationships and Drug Design

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Quantitative Aspects of Drug-Receptor Interaction01:30

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Quantitative Structure-Activity Relationship, Activity Prediction, and Molecular Dynamics of Non-nucleotide Reverse Transcriptase Inhibitors
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Quantitative Structure-Activity Relationship, Activity Prediction, and Molecular Dynamics of Non-nucleotide Reverse Transcriptase Inhibitors

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Molecular modeling on structure-function analysis of human progesterone receptor modulators.

Ria Pal1, Md Ataul Islam, Tabassum Hossain

  • 1Department of Chemical Technology, University of Calcutta, 92, A.P.C. Road, Kolkata-700009, India.

Scientia Pharmaceutica
|September 3, 2011
PubMed
Summary

This study identifies key molecular features for selective progesterone receptor-A binding using QSAR and pharmacophore modeling. These insights guide the design of novel progesterone receptor (PR) modulators.

Keywords:
Binding affinityDockingHuman progesterone receptor-APharmacophore mappingQSARQuinoline and cyclocymopol monomethyl ether derivatives

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Published on: August 16, 2018

Area of Science:

  • Medicinal Chemistry
  • Computational Chemistry
  • Pharmacology

Background:

  • Progesterone receptor (PR) modulators are significant therapeutic agents.
  • Selective targeting of PR subtypes, particularly PR-A, is crucial for therapeutic efficacy and minimizing side effects.
  • Understanding the structural basis of ligand-receptor interactions is essential for drug design.

Purpose of the Study:

  • To elucidate the biophoric signals governing selective binding to progesterone receptor subtype-A (PR-A).
  • To develop predictive models for designing nonsteroidal PR modulators based on quinoline and cyclocymopol monomethyl ether derivatives.
  • To characterize structure-function relationships for ligand-PR-A interactions.

Main Methods:

  • Ligand-based quantitative structure-activity relationship (QSAR) studies were performed on 100 training, 30 test, and 40 validation set compounds.
  • Receptor-independent pharmacophore space modeling was conducted using training (n=26), test (n=60), and validation (n=84) sets.
  • Receptor-based docking studies were employed for structure-function characterization and validation of identified molecular attributes.

Main Results:

  • Consensus QSAR models revealed that molecular topology, atomic properties (polarizability, electronegativity), atomic mass, and van der Waals volume, along with functional atoms (F, Cl, N, O), significantly influence ligand binding affinity to PR-A.
  • Pharmacophore modeling highlighted the importance of aromatic rings, hydrogen bond donors, molecular hydrophobicity, and steric factors for effective receptor binding.
  • Docking studies confirmed the role of these mapped molecular attributes in ligand-receptor interactions within the PR-A catalytic cleft.

Conclusions:

  • The study successfully identified critical molecular descriptors and pharmacophoric features essential for selective PR-A binding.
  • These findings provide a strong foundation for the rational design and optimization of novel, nonsteroidal PR-A modulators.
  • The integrated approach of QSAR, pharmacophore modeling, and docking offers valuable insights into ligand-PR interactions for drug discovery.