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Structural Modifications of Salicylates: Inhibitors of Human CD81‐Receptor HCV‐E2 Interaction
Author(s) -
Holzer Marcel,
Ziegler Sigrid,
Neugebauer Alexander,
Kronenberger Bernd,
Klein Christian D.,
Hartmann Rolf W.
Publication year - 2008
Publication title -
archiv der pharmazie
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 61
eISSN - 1521-4184
pISSN - 0365-6233
DOI - 10.1002/ardp.200700261
Subject(s) - cd81 , chemistry , protein data bank (rcsb pdb) , virtual screening , receptor , stereochemistry , biochemistry , hepatitis c virus , virology , drug discovery , virus , biology
Starting point of the present paper was the result of a virtual screening using the open conformation of the large extracellular loop (LEL) of the CD81‐receptor (crystal structure: PDB‐ID: 1G8Q). After benzyl salicylate had been experimentally validated to be a moderate inhibitor of the CD81‐LEL–HCV‐E2 interaction, further optimization was performed and heterocyclic‐substituted benzyl salicylate derivatives were synthesized. The compounds were tested for their ability to inhibit the interaction of a fluorescence‐labeled antibody to CD81‐LEL using HUH7.5 cells. No compound showed an increase concerning the inhibition of the protein‐protein interaction compared to benzyl salicylate.

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