Mechanism of action<unk>  works by disrupting the HIV-1 molecular machinery at the final stage of fusion with the target cell, preventing uninfected cells from becoming infected. A biomimetic peptide,<unk>  was designed to mimic components of the HIV-1 fusion machinery and displace them, preventing normal fusion. Drugs that disrupt fusion of virus and target cell are termed entry inhibitors or fusion inhibitors. HIV binds to the host CD4+ cell receptor via the viral protein gp120; gp41, a viral transmembrane protein, then undergoes a conformational change that assists in the fusion of the viral membrane to the host cell membrane.<unk>  binds to gp41 preventing the creation of an entry pore for the capsid of the virus, keeping it out of the cell.<unk>  is also an activator of the chemotactic factor receptor, formyl peptide receptor 1, and thereby activates phagocytes and presumably other cells bearing this receptor (see formyl peptide receptors). The physiological significance of this activation is unknown. Microbiology<unk>  is considered to be active against HIV-1 only. Low activity against HIV-2 isolates has been demonstrated in vitro. Variable susceptibility to<unk>  has been observed in clinical isolates, with acquired resistance the result of a mutated 10 amino acid motif in viral gp41. Primary resistance, however, has yet to be observed.
Enfuvirtide
Saquinavir
Coronavir
Abacavir
Indinavir
Fosamprenavir
Entecavir
Amprenavir