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-piperidinecarboxylic acid) converted the substrate into an effective inhibitor of HIV-1 and HIV-2 proteinases with IC50 of ∼ 1 μM. This compound showed a high degree of selectivity in that it did not inhibit cathepsin D and renin.
|Number of pages||5|
|Journal||Biochemical and biophysical research communications|
|Publication status||Published - May 31 1990|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology