Fluorescence-based continuous assay for the aspartyl protease of human immunodeficiency virus-1
- 12 March 1990
- journal article
- Published by Wiley in FEBS Letters
- Vol. 262 (1) , 119-122
- https://doi.org/10.1016/0014-5793(90)80168-i
Abstract
5-Dimethylaminonaphthalene-1-sulfonyl-Ser-Gln-Asn-Tyr-Pro-Ile-Val-Trp (Dns-SQNYPIVW) is a fluorescent substrate for the aspartyl protease of human immunodeficiency virus-1. In intact substrate, fluorescence of Trp (λ ex 290 nm, λ em 360 nm) was 60% quenched by energy transfer to the dansyl group. Protease-catalyzed cleavage at the Tyr-Pro bond abolished the energy transfer, and the consequent increase in Trp fluorescence was used to follow the enzymatic reaction. At substrate concentrations 100 μM.Keywords
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