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A Selective HIV-Protease Assay Based on a Chromogenic Amino Acid

✍ Scribed by Fabrizio Badalassi; Hong Khan Nguyen; Paolo Crotti; Jean-Louis Reymond

Publisher
John Wiley and Sons
Year
2002
Tongue
German
Weight
146 KB
Volume
85
Category
Article
ISSN
0018-019X

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✦ Synopsis

Dedicated to Professor Dieter Seebach on the occasion of his 65th birthday (2S,3S)-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 sequencespecific chromogenic protease substrates when used in the presence of NaIO 4 and bovine serum albumin. The peptide 1 (KRAVNleÀ5ÀEANleNH 2 (Nle norleucine)) allows detection of HIV-protease activity spectrophotometrically at 405 nm.

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HIV-1 protease cleavage site prediction based on amino acid property
✍ Bing Niu; Lin Lu; Liang Liu; Tian Hong Gu; Kai-Yan Feng; Wen-Cong Lu; Yu-Dong Ca 📂 Article 📅 2009 🏛 John Wiley and Sons 🌐 English ⚖ 527 KB

## Abstract Knowledge of the polyprotein cleavage sites by HIV protease will refine our understanding of its specificity, and the information thus acquired is useful for designing specific and efficient HIV protease inhibitors. Recently, several works have approached the HIV‐1 protease specificity