Substitution of proline with pipecolic acid at the scissile bond converts a peptide substrate of HIV proteinase into a selective inhibitor.

@article{Copeland1990SubstitutionOP,
  title={Substitution of proline with pipecolic acid at the scissile bond converts a peptide substrate of HIV proteinase into a selective inhibitor.},
  author={Terry D. Copeland and E M Wondrak and J{\'o}zsef Tőzs{\'e}r and Marion M Roberts and Stephen Oroszlan},
  journal={Biochemical and biophysical research communications},
  year={1990},
  volume={169 1},
  pages={310-4}
}
The nonapeptide H-Val-Ser-Gln-Asn-Tyr-Pro-Ile-Val-Gln-NH2 containing the retroviral Tyr-Pro cleavage site is a good substrate for the proteinase of human immunodeficiency viruses but it is not readily hydrolyzed by other nonviral proteinases including the structurally related pepsin-like aspartic proteinases. Replacing the Pro by L-pipecolic acid (2… CONTINUE READING