Small dipeptide-based HIV protease inhibitors containing the hydroxymethylcarbonyl isostere as an ideal transition-state mimic.

@article{Kiso1999SmallDH,
  title={Small dipeptide-based HIV protease inhibitors containing the hydroxymethylcarbonyl isostere as an ideal transition-state mimic.},
  author={Y. Kiso and H. Matsumoto and S. Mizumoto and T. Kimura and Y. Fujiwara and K. Akaji},
  journal={Biopolymers},
  year={1999},
  volume={51 1},
  pages={
          59-68
        }
}
  • Y. Kiso, H. Matsumoto, +3 authors K. Akaji
  • Published 1999
  • Chemistry, Medicine
  • Biopolymers
  • The human immunodeficiency virus (HIV) codes for an aspartic protease known to be essential for retroviral maturation and replication. HIV protease is formed from two identical 99 amino acid peptides. We synthesized [(NHCH2CH2-S-CH2CO)51-52, Ala67,95]HIV-1 protease using the thioether chemical ligation method, and then prepared the [(NHCH2CH2-S-CH2CO)51-52, Ala67,95, Cys98]HIV-1 protease dimer analogue covalently linked by a disulfide bridge. These HIV-1 protease analogues effectively cleaved… CONTINUE READING
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