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  • Technician
  • Undergraduate Student
  • Veterinary
  • Visiting Scientist
  • Deputy Director of Center
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  • Deputy Director of National Reference Center
  • Deputy Head of Facility
  • Director of Center
  • Director of Department
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© Research
Publication : Chemical science

Pharmacomodulation of a ligand targeting the HBV capsid hydrophobic pocket.

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Chemical science - 04 Aug 2022

Briday M, Hallé F, Lecoq L, Radix S, Martin J, Montserret R, Dujardin M, Fogeron ML, Nassal M, Meier BH, Lomberget T, Böckmann A

Link to Pubmed [PMID] – 36042894

Link to DOI – 10.1039/d2sc02420a

Chem Sci 2022 Aug; 13(30): 8840-8847

Hepatitis B virus (HBV) is a small enveloped retrotranscribing DNA virus and an important human pathogen. Its capsid-forming core protein (Cp) features a hydrophobic pocket proposed to be central notably in capsid envelopment. Indeed, mutations in and around this pocket can profoundly modulate, and even abolish, secretion of enveloped virions. We have recently shown that Triton X-100, a detergent used during Cp purification, binds to the hydrophobic pocket with micromolar affinity. We here performed pharmacomodulation of pocket binders through systematic modifications of the three distinct chemical moieties composing the Triton X-100 molecule. Using NMR and ITC, we found that the flat aromatic moiety is essential for binding, while the number of atoms of the aliphatic chain modulates binding affinity. The hydrophilic tail, in contrast, is highly tolerant to changes in both length and type. Our data provide essential information for designing a new class of HBV antivirals targeting capsid-envelope interactions.