HIV Protease Substrates and inhibitors

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CAT# Product Name M.W Molecular Formula Inquiry
HB00138 H-Ser-Gln-Asn-Tyr-Pro-Ile-Val-OH 819.91 C37H57N9O12 Inquiry
HB00140 H-Ser-Gln-Asn-Phe-psi(CH2NH)Pro-Ile-Val-Gln-OH 918.06 C42H67N11O12 Inquiry
HB00141 DABCYL-γ-Abu-Ser-Gln-Asn-Tyr-Pro-Ile-Val-Gln-EDANS trifluoroacetate salt 1532.74 C73H97N17O18S Inquiry
HB00143 HIV Protease Substrate VII 1140.31 C52H81N15O14 Inquiry
HB00144 HIV Protease Substrate IV 1090.29 C49H83N15O13 Inquiry
HB00145 Ac-Thr-Ile-Nle-psi(CH₂NH)Nle-Gln-Arg-NH₂ 769.99 C35H67N116O8 Inquiry
HB00146 Ac-Ser-Gln-Asn-Tyr-OH 552.54 C23H32N6O10 Inquiry
HB00147 HIV Protease Substrate VI 891.04 C40H66N12O11 Inquiry
HB00148 Anthranilyl-HIV Protease Substrate trifluoroacetate salt 940.07 C43H65N13O11 Inquiry
HB00149 Ac-Thr-Leu-Asn-Phe-OH 535.6 C25H37N5O8 Inquiry
HB00150 HIV Protease Substrate III 1314.51 C58H95N19O16 Inquiry
HB00151 Anthranilyl-HIV Protease Substrate III trifluoroacetate salt 1433.63 C65H100N20O17 Inquiry
HB00152 Ac-Thr-Val-Ser-Phe-Asn-Phe-OH trifluoroacetate salt 755.83 C36H49N7O11 Inquiry
HB00153 Ac-Leu-Val-Phe-aldehyde 403.52 C22H33N3O4 Inquiry
HB00154 H-Arg-Val-Leu-psi(CH2NH)Phe-Glu-Ala-Nle-NH2 832.06 C40H69N11O8 Inquiry
HB00155 H-His-Cys-Lys-Phe-Trp-Trp-OH 906.08 C46H55N11O7S Inquiry
HB00156 HIV Protease Substrate III-B (Native Sequence) 1211.46 C51H90N18O14S Inquiry
HB00157 Anthranilyl-HIV Protease Substrate V trifluoroacetate salt 1081.24 C50H76N14O13 Inquiry

HIV-1 protease (PR) is a retrovirus aspartate protease (retrovirus pepsin), an enzyme that hydrolyzes peptide bonds in retroviruses. The life cycle of HIV (the retrovirus that causes AIDS) is essential. HIV protease decomposes the newly synthesized polyproteins (i.e. Gag and Gag-Pol) to produce the mature protein components of HIV virus particles at nine cleavage sites, that is, the infection form of the virus outside the host cells. In the absence of an effective HIV protease, HIV virus particles are still non-communicable.

Introduction of HIV Protease Substrates

The oligopeptide containing the consistent retrovirus protease cleavage sequence Ser/Thr-X-Y-Tyr/Phe-Pro is the substrate of the purified recombinant HIV-1 protease. Replacing the lysed dipeptide with reduced Phe-Pro or Tyr-Pro dipeptide alleles or statins compound 3-hydroxy-4-amino-5-phenylvaleric acid, a HIV-1 protease inhibitor with Ki value in the range of micromoles can be obtained by replacing the lysed dipeptide with reduced HIV-1 or HIV-1 dipeptide allele or statins compound 3-hydroxy-4-amino-5-phenylvaleric acid. The affinity of the substrate was three orders of magnitude higher than that of the corresponding substrate. HIV-1 protease inhibitors may provide a new and potential treatment for AIDS.

Designs of HIV protease inhibitors

HIV-1 protease plays an important role in the life cycle of HIV. Like many other viruses, HIV can string its many proteins together to form a long chain. HIV-1 protease, on the other hand, can cut polyproteins into protein fragments of appropriate length, and the timing of this step is crucial. Protease inhibitors can irreversibly occupy the space between enzyme and substrate, so that HIV protease can’t bind to the substrate and hydrolyze the corresponding peptide bond, thus inhibiting the synthesis of functional enzymes and structural proteins needed for the assembly of new viruses. The first HIV protease inhibitor was Saquinavir, produced by Roche in 1995. Then, on March 1, 1996, Ritonavir was also licensed by FDA in the United States. On March 13, 1996, Mercadon Pharmaceuticals’s Indinavir was marketed as the third new HIV protease inhibitor. The FDA-approved HIV protease inhibitors share same structural similarities and a similar binding pattern, which may cause some of the common side effects of the protease inhibitor-containing regimens.

Future of HIV Protease Inhibitors

Several new HIV protease inhibitors are undergoing clinical trials. Before the new HIV protease inhibitor stent eliminates the non-targeting effect, the development of HIV protease inhibitor prodrug can reduce the drug dosage and improve the adverse drug reactions. With the accumulation of knowledge about the toxic chemical groups of HIV protease inhibitors, the “benign chemical library” of HIV protease inhibitors can be compiled, which is beneficial to the drug design and research in the future.

References

  1. Lv, Z., Chu, Y., & Wang, Y. (2015). HIV protease inhibitors: a review of molecular selectivity and toxicity. HIV/AIDS (Auckland, NZ), 7, 95.
  2. Patel, P., & Louie, S. (2018). Drug Interactions in HIV: Protease and Integrase Inhibitors. In Drug Interactions in Infectious Diseases: Antimicrobial Drug Interactions (pp. 255-295). Humana Press, Cham.
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