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Antivirals for allosteric inhibition of Zika virus using a homology model and experimentally determined structure of envelope protein.

Sandun D FernandoTeshan Fernando
Published in: BMC research notes (2017)
By examining how glycan molecules, small-molecule probes and screened ligands that have a high affinity to ZVEP, we report the mechanics of ZVEP to inhibition via allosteric blockage of the glycan-binding domain while proposing even more possibly potent inhibitors. The small molecular probes based study using the homology model and subsequently verified using actual experimental structure, 5IRE, revealed that ZVEP is druggable. A pharmacophore analysis followed by screening showed at least four ligands that allosterically binds to the glycan binding domain constituted by residues VAL 153 and ASN 154 in 5IRE. Based on further selection criteria ZINC40621658 was identified to have high potential to be a strong antiviral candidate for Zika virus inhibition.
Keyphrases
  • zika virus
  • small molecule
  • protein protein
  • dengue virus
  • aedes aegypti
  • endoplasmic reticulum stress
  • cell surface
  • binding protein
  • single molecule
  • living cells
  • molecular dynamics
  • risk assessment
  • transcription factor