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Novel Insight into Inhibitor Binding of Highly Symmetric HIV‐1 Protease
Author(s) -
Wollmann Jörg,
Baumert Christiane,
Erlenkamp German,
Sippl Wolfgang,
Hilgeroth Andreas
Publication year - 2008
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200700646
Subject(s) - hiv 1 protease , protease , chemistry , hydrogen bond , docking (animal) , stereochemistry , enzyme , binding site , human immunodeficiency virus (hiv) , enzyme inhibitor , protease inhibitor (pharmacology) , biochemistry , combinatorial chemistry , virology , biology , organic chemistry , molecule , medicine , nursing , antiretroviral therapy , viral load
HIV‐1 protease inhibitor binding . Inhibitor binding towards HIV‐1 protease subsites was investigated by the introduction of hydrogen bond acceptor and donor functions into the phenylic substituents of cage dimeric 1,4‐dihydropyridines. Determined affinity constants K i are discussed and suggested binding modes towards enzyme′s subsites are confirmed by docking studies.