In silico identification and screening of CYP24A1 inhibitors: 3D QSAR pharmacophore mapping and molecular dynamics analysis

J Biomol Struct Dyn. 2019 Apr;37(7):1700-1714. doi: 10.1080/07391102.2018.1464958. Epub 2018 May 4.

Abstract

Vitamin D is a key signalling molecule that plays a vital role in the regulation of calcium phosphate homeostasis and bone remodelling. The circulating biologically active form of vitamin D is regulated by the catabolic mechanism of cytochrome P450 24-hydroxylase (CYP24A1) enzyme. The over-expression of CYP24A1 negatively regulates the vitamin D level, which is the causative agent of chronic kidney disease, osteoporosis and several types of cancers. In this study, we found three potential lead molecules adverse to CYP24A1 through structure-based, atom-based pharmacophore and e-pharmacophore-based screening methods. Analysis was done by bioinformatics methods and tools like binding affinity (binding free energy), chemical reactivity (DFT studies) and molecular dynamics simulation (protein-ligand stability). Combined computational investigation showed that the compounds NCI_95001, NCI_382818 and UNPD_141613 may have inhibitory effects against the CYP24A1 protein.

Keywords: screening; CYP24A1; DFT analysis; molecular dynamics; vitamin D.

MeSH terms

  • Animals
  • Binding Sites
  • Density Functional Theory
  • Enzyme Inhibitors / chemistry*
  • Enzyme Inhibitors / pharmacology
  • Humans
  • Hydrogen Bonding
  • Ligands
  • Molecular Docking Simulation*
  • Molecular Dynamics Simulation*
  • Molecular Structure
  • Protein Binding
  • Quantitative Structure-Activity Relationship*
  • Rats
  • Reproducibility of Results
  • Vitamin D3 24-Hydroxylase / antagonists & inhibitors
  • Vitamin D3 24-Hydroxylase / chemistry*

Substances

  • Enzyme Inhibitors
  • Ligands
  • CYP24A1 protein, human
  • Vitamin D3 24-Hydroxylase