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Front Cover: Design of Highly Potent, Dual‐Acting and Central‐Nervous‐System‐Penetrating HIV‐1 Protease Inhibitors with Excellent Potency against Multidrug‐Resistant HIV‐1 Variants (ChemMedChem 8/2018)
Author(s) -
Ghosh Arun K.,
Rao Kalapala Venkateswara,
Nyalapatla Prasanth R.,
Kovela Satish,
Brindisi Margherita,
Osswald Heather L.,
Sekhara Reddy Bhavanam,
Agniswamy Johnson,
Wang YuanFang,
Aoki Manabu,
Hattori Shinichiro,
Weber Irene T.,
Mitsuya Hiroaki
Publication year - 2018
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.201800226
Subject(s) - darunavir , ligand (biochemistry) , human immunodeficiency virus (hiv) , chemistry , stereochemistry , front cover , hiv 1 protease , potency , protease , cover (algebra) , biochemistry , virology , biology , antiretroviral therapy , enzyme , in vitro , receptor , mechanical engineering , engineering , viral load
The Front Cover displays the overlay of the protein–ligand X‐ray structure of an exceptionally potent inhibitor GRL‐14213‐bound HIV‐1 protease. The crown‐like structural architecture of the new P2 ligand has been designed to both maintain the key “backbone binding” interactions similar to darunavir, as well as to make enhanced van der Waals interactions in the active site. The inhibitor also incorporates an aminobenzothiazole as the P2’‐ligand. The Boilermaker Statue of Purdue University (left) exemplifies an inspirational structural architecture. Art credit: Mr. Steve Scherer. More information can be found in the Full Paper by Arun K. Ghosh et al. on page 803 in Issue 8, 2018 (DOI: 10.1002/cmdc.201700824).