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Cover Picture: Probing Multidrug‐Resistance and Protein–Ligand Interactions with Oxatricyclic Designed Ligands in HIV‐1 Protease Inhibitors (ChemMedChem 11/2010)
Author(s) -
Ghosh Arun K.,
Xu ChunXiao,
Rao Kalapala Venkateswara,
Baldridge Abigail,
Agniswamy Johnson,
Wang YuanFang,
Weber Irene T.,
Aoki Manabu,
Miguel Salcedo Gomez Pedro,
Amano Masayuki,
Mitsuya Hiroaki
Publication year - 2010
Publication title -
chemmedchem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 0.817
H-Index - 100
eISSN - 1860-7187
pISSN - 1860-7179
DOI - 10.1002/cmdc.201090049
Subject(s) - darunavir , ligand (biochemistry) , chemistry , stereochemistry , protease , human immunodeficiency virus (hiv) , combinatorial chemistry , biochemistry , biology , virology , antiretroviral therapy , receptor , enzyme , viral load
The cover picture shows the overlay of the protein–ligand X‐ray structures of darunavir and saquinivir‐bound HIV‐1 protease. This structural architecture provided the inspiration for a new tris‐THF ligand that would both maintain the “backbone binding” interactions of darunavir, as well as fill the S3 subsite comparable to saquinavir. GRL‐0519A contains a stereochemically defined syn‐anti‐syn architecture in the P2 ligand. The Purdue University Bell Tower (shown on the right‐hand side) also exemplifies a beautiful and functional structural architecture. It has long been a symbol of the will to ever strive for that next greater achievement. For more details, see the Communication by Arun K. Ghosh et al. on p. 1850 ff. Cover art credit to: Dr. Xiaoming Xu and Mr. Steve Scherer.