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The novel synthesis of the protease inhibitor (S)‐1‐chloro‐3‐[(p‐tolylsulfonyl)amino]‐7‐amino‐2‐[5,5,6,6‐ 3 H]heptanone ([ 3 H]TLCK) labeled to high specific activity with tritium
Author(s) -
Villani A. J.,
Heys J. R.
Publication year - 1997
Publication title -
journal of labelled compounds and radiopharmaceuticals
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.432
H-Index - 47
eISSN - 1099-1344
pISSN - 0362-4803
DOI - 10.1002/(sici)1099-1344(199705)39:5<379::aid-jlcr981>3.0.co;2-i
Subject(s) - chemistry , tritium , stereospecificity , hydrolysis , amino acid , yield (engineering) , protease , hexanoic acid , stereochemistry , protease inhibitor (pharmacology) , specific activity , enzyme , medicinal chemistry , organic chemistry , catalysis , biochemistry , physics , materials science , human immunodeficiency virus (hiv) , antiretroviral therapy , nuclear physics , viral load , metallurgy , medicine , family medicine
The protease inhibitor (S)‐1‐chloro‐3‐[(p‐tolylsulfonyl)amino]‐7‐amino‐2‐[5,5,6,6‐ 3 H]heptanone ([ 3 H]TLCK) was prepared in an overall 41% radiochemical yield with a specific activity of 1.6 Ci/mmol in a ‘one‐pot’ 3 step sequence beginning with (S)‐6‐[[(1,1‐dimethylethyl)oxy]carbonyl]‐2‐(p‐tolylsulfonyl)amino[4,4,5,5‐ 3 H]hexanoic acid. The latter was prepared with a specific activity of 123 Ci/mmol in a 3 step sequence beginning with the stereospecific enzymatic hydrolysis of the commercially available racemic 2‐acetylamino‐6‐[[(1,1‐dimethylethyl)‐oxy]carbonyl]aminohexan‐4‐ynoic acid, followed by tosylation and then palladium catalyzed reduction of the triple bond under tritium. © 1997 John Wiley & Sons, Ltd.