| Autor: |
Toth MV; Department of Pharmacology, Washington University School of Medicine, St. Louis, Missouri., Marshall GR |
| Jazyk: |
angličtina |
| Zdroj: |
International journal of peptide and protein research [Int J Pept Protein Res] 1990 Dec; Vol. 36 (6), pp. 544-50. |
| DOI: |
10.1111/j.1399-3011.1990.tb00994.x |
| Abstrakt: |
Novel fluorogenic substrates for human immunodeficiency viral protease have been developed based on the principle of fluorescence energy transfer. Starting from a p24/p15 cleavage site-derived hexapeptide substrate. Ac-Thr-Ile-Nle-Nle-Gln-Arg-NH2, incorporation of 2-aminobenzoic acid in place of the acetyl group as the donor and p-NO2-Phe at the P1' position as acceptor gave the intramolecularly quenched fluorogenic substrate. Cleavage of the substrate by HIV protease released the fluorescent N-terminal tripeptide from its close apposition to the quenching nitrobenzyl group, resulting in enhanced fluorescence. An automated assay based on 96-well microtiter plates and a fluorometric plate reader have been developed, which allow high throughput of compounds in the search for HIV protease inhibitors. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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