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A Selective HIV‐Protease Assay Based on a Chromogenic Amino Acid
Author(s) -
Badalassi Fabrizio,
Nguyen Hong Khan,
Crotti Paolo,
Reymond JeanLouis
Publication year - 2002
Publication title -
helvetica chimica acta
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.74
H-Index - 82
eISSN - 1522-2675
pISSN - 0018-019X
DOI - 10.1002/1522-2675(200210)85:10<3090::aid-hlca3090>3.0.co;2-8
Subject(s) - chemistry , chromogenic , norleucine , protease , bovine serum albumin , hiv 1 protease , peptide , oligopeptide , amino acid , human immunodeficiency virus (hiv) , derivative (finance) , chromatography , biochemistry , stereochemistry , enzyme , virology , methionine , financial economics , economics , biology
(2 S ,3 S )‐2‐Amino‐3‐hydroxy‐5‐(4‐nitrophenoxy)pentanoic acid ( 5 ) was prepared stereoselectively as the N ‐Fmoc, O ‐( tert ‐butyl)‐protected derivative 5a in eleven steps from ethyl ( E )‐4‐benzyloxypent‐2‐enoate ( 6 ). This protected amino acid was used for the solid‐phase peptide synthesis of oligopeptides, which serve as sequence‐specific chromogenic protease substrates when used in the presence of NaIO 4 and bovine serum albumin. The peptide 1 (KRAVNle 5 EANleNH 2 (Nle=norleucine)) allows detection of HIV‐protease activity spectrophotometrically at 405 nm.