z-logo
Premium
Synthesis of deuterium‐labelled 5′‐ O ‐[ N ‐(Salicyl)sulfamoyl]adenosine (Sal‐AMS‐d 4 ) as an internal standard for quantitation of Sal‐AMS
Author(s) -
Gupte Amol,
Subramanian Murali,
Remmel Rory P.,
Aldrich Courtney C.
Publication year - 2008
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/jlcr.1490
Subject(s) - chemistry , microsome , stereochemistry , in vivo , adenosine , enzyme , biochemistry , microbiology and biotechnology , biology
5′‐ O ‐[ N ‐(Salicyl)sulfamoyl]adenosine (Sal‐AMS, 1) is a potent inhibitor of the bifunctional enzyme salicyl‐AMP ligase in Mycobacterium tuberculosis . This inhibitor acts by disrupting the biosynthesis of the mycobactin siderophores that are essential for the process of iron acquisition. To aid with in vitro metabolism and in vivo pharmacokinetic studies of Sal‐AMS, a stable deuterium‐labelled Sal‐AMS analog (Sal‐AMS‐d 4 ) was synthesized. This deuterium‐labelled analog was used as an internal standard to conduct in vitro plasma and microsomal stability studies. Sal‐AMS was found to be stable for 24 h in human plasma and 1 h in human liver microsomes at 37°C. Copyright © 2008 John Wiley & Sons, Ltd.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here