is it possible for HIV protease inhibitors to affect cellular protease?
HIV protease inhibitors are peptide-like chemicals that competitively inhibit the action of the virus aspartyl protease.
These aspartyl proteases are specific to the retroviruses and differ from eukaryotic proteases.
Hence HIV protease inhibitors won't affect the cellular proteases..
is it possible for HIV protease inhibitors to affect cellular protease?
Drugs that are HIV protease inhibitors Multiple Choice prevent HIV protease from degrading host cell proteins О block the translation of HIV proteases bind to HIV proteases prevent HIV proteases from breaking apart capsid proteins bind to HIV proteases and prevent the proteases from breaking apart capsid proteins
Many patients become resistant to HIV protease inhibitors with the passage of time owing to mutations in the HIV gene that encodes the protease. Provide a detailed rationale for the observation that mutations are not found in the active site aspartate residues.
14. HIV-1 Protease is an enzyme made by HIV that hydrolyzes the long viral polyprotein into their functional protein components. HIV patients are treated with inhibitors of HIV Protease, which in turn inhibit HIV replication. Two competitive inhibitors of HIV-1 Protease are saquinavir (K = 0.40 nM) and ritonavir (K1 = 0.015 nM). (K, are dissociation constants for the reaction IE + I + E, where I is the inhibitor and E is HIV Protease.) a) Which would have a...
how do protease inhibitors work?
The HIV protease structure was solved very early in the process of developing anti-HIV drugs. Importantly, the protease was found to be quite similar to proteases like chymotrypsin and trypsin. Compare and contrast the catalytic mechanism and binding properties of chymotrypsin, trypsin, and the HIV protease.
7. The HIV protease structure was solved very early in the process of developing anti-HIV drugs Importantly, the protease was found to be quite similar to proteases like chymotrypsin and trypsin. Compare and contrast the catalytic mechanism and binding properties of chymotrypsin trypsin, and the HIV protease.
The HIV-1 protease is a member of a conserved family of enzymes. A related protease is found in Rous Sarcoma Virus. A portion of each sequence is shown above, with the catalytic residue highlighted. Looking at amino acids 20-30 for two protease sequences, what is the percent identity?
7. The HIV protease structure was solved very early in the process of developing anti-HIV drugs. Importantly, the protease was found to be quite similar to proteases like chymotrypsin and trypsin. Compare and contrast the catalytic mechanism and binding properties of chymotrypsin, trypsin, and the HIV protease. Catalitic mechanism chymotryps in this enzyme help digest and works in the intestine to help Break down Large protein molecules
There is a new strain of HIV that has an atypical enzyme structure. As such, none of the current inhibitors are effective against the HIV protease [Essential Biochemistry (p206, 3rd edition); (p198, 4th edition)]. You are charged with developing a new inhibitor for this new HIV strain with different protease. 1. Describe how you can design an inhibitor for this HIV protease. 2. How can you test the inhibitor for biologic effect?
sdent ork 10/27/17 50% 1st attempt Structure-based drug design strategies often devise competitive Inhibitors that bind to certain enzyme active sites. For example saquinavir and Indinavir are designed HIV protease inhibitors that bind to the aspartate protease enzyme of HIV, which is required for the virus to produce functional proteins for further HIV infection. Which of the following statements are true about saquinavir and Indinavir? Choose one or more: A. Very high local concentrations of proteins with Phe-Pro or Tyr-Pro...