- High efficiency antiretroviral therapy is to treat AIDS through the combination of a variety of antiviral drugs
- Some peptides targeting HIV envelope glycoprotein (Env) can effectively inhibit HIV infection.
- Further mechanism studies showed that f9170 targeted the llp1 domain of HIV-1 envelope glycoprotein, and then formed hydrophilic channel on the envelope protein of HIV-1, which released the viral genome and eventually led to the virus losing the ability to infect.
High efficiency antiretroviral therapy is to treat AIDS through the combination of a variety of antiviral drugs
which can inhibit the replication of HIV to the maximum extent, and gradually restore the damaged immune function of patients, so as to delay the progression of the disease and prolong the life of patients, so as to win more time for the treatment of AIDS patients. However, there will always be viruses that escape the drug hunt, and the treatment does not completely eliminate HIV.
In addition, once the antiviral drug treatment is stopped, HIV can come back to the level before treatment, and the rebound of HIV will become the “killer” of human infection again. In addition, anti HIV drugs, especially single anti HIV drugs, can induce the emergence of HIV resistant virus strains in clinical use, which greatly limits the long-term use of antiviral drugs. The development of HIV inhibitors targeting new targets will be the development direction of drug resistance instead of existing drugs.
Some peptides targeting HIV envelope glycoprotein (Env) can effectively inhibit HIV infection.
Based on this, a peptide library targeting HIV envelope protein and a peptide targeting HIV transmembrane protein gp41, named f9170, was obtained from the library. F9170 can effectively inactivate HIV and induce necrosis of HIV infected cells.
The peptide can activate latent infection cells and induce cell necrosis. F9170 did not appear to have toxicity or immunogenicity in mice treated with f9170. The results of drug distribution in vivo showed that f9170 could penetrate mouse brain and lymph node tissues with HIV latent pool. In rhesus monkeys with chronic SHIV infection, the viral load can be controlled below the detection limit by using f9170 for a short period of time.
Further mechanism studies showed that f9170 targeted the llp1 domain of HIV-1 envelope glycoprotein, and then formed hydrophilic channel on the envelope protein of HIV-1, which released the viral genome and eventually led to the virus losing the ability to infect.
The mechanism of action of f9170 is different from other antiviral drugs, not by inhibiting the physiological effect of the target, but by interacting with the target to destroy the integrity of cell membrane. F9170 can effectively activate dormant virus together with HIV latent library activator.
At the same time, f9170 can induce the necrosis of HIV infected cells and HIV infected cells after activation. F9170 is expected to become a candidate drug for AIDS treatment, but it needs continuous basic research before it can be applied in clinical practice.
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