Rational Drug Design Approach to Synthesizing HIV-1 Protease Inhibitors
... studies have also characterized cleavage site mutants. Since mutations at the active site can affect the rate at which the Gag and Gag/Pol protein precursors are cleaved by the protease, one can imagine that mutations at the cleavage site of these respective protein precursors could compensate for r ...
... studies have also characterized cleavage site mutants. Since mutations at the active site can affect the rate at which the Gag and Gag/Pol protein precursors are cleaved by the protease, one can imagine that mutations at the cleavage site of these respective protein precursors could compensate for r ...
An Overview of HIV Drugs
... Closer Look: Maraviroc 1st oral entry inhibitor Blocks coreceptor CCR5 Resistance from one or more of several mutations in the V3 loop of gp120 or gp160 Possible Side Effects: Cough, Fever, Dizziness, Headache, Lowered BP, Nausea, and Bladder Irritation ...
... Closer Look: Maraviroc 1st oral entry inhibitor Blocks coreceptor CCR5 Resistance from one or more of several mutations in the V3 loop of gp120 or gp160 Possible Side Effects: Cough, Fever, Dizziness, Headache, Lowered BP, Nausea, and Bladder Irritation ...
Anti-HIV Drugs
... or inhibitors at the substrate binding site of RT • NRTI’s must be phosphorylated (three steps) to their 5’-triphosphate form to become active inhibitors. • Nucleotide analogs (NtRTI) already contain a phosphate group and only go through 2 steps to become active. • The 5’-triphosphate of the NRTI’s ...
... or inhibitors at the substrate binding site of RT • NRTI’s must be phosphorylated (three steps) to their 5’-triphosphate form to become active inhibitors. • Nucleotide analogs (NtRTI) already contain a phosphate group and only go through 2 steps to become active. • The 5’-triphosphate of the NRTI’s ...
Discovery and development of HIV-protease inhibitors
Many major physiological processes depend on regulation of proteolytic enzyme activity and there can be dramatic consequences when equilibrium between an enzyme and its substrates is disturbed. In this prospective, the discovery of small-molecule ligands, like protease inhibitors, that can modulate catalytic activities has an enormous therapeutic effect. Hence, inhibition of the HIV protease is one of the most important approaches for the therapeutic intervention in HIV infection and their development is regarded as major success of structure-based drug design. They are highly effective against HIV and have, since the 1990s, been a key component of anti-retroviral therapies for HIV/AIDS.