Covalent binding of nitrogen mustards to the cysteine-34 residue in human serum albumin

article


Noort, D.

Hulst, A.G.

Jansen, R.
Covalent binding of various clinically important nitrogen mustards to the cysteine-34 residue of human serum albumin, in vitro and in vivo, is demonstrated. A rapid method for detection of these adducts is presented, based on liquid chromatography-tandem mass spectrometry analysis of the adducted tripeptide Cys*-Pro-Phe after digestion of the protein with Pronase.
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AdductsAlbuminBiomonitoringChemotherapyNitrogen mustardsTandem mass spectrometryChlorambucilChlormethineChlormethine derivativeDichlorodiethylamineHuman serum albuminPhenylalanineProlinePronaseTripeptideAmino acid analysisControlled studyCovalent bondDrug protein bindingIn vitro studyIn vivo studyLiquid chromatographyTandem mass spectrometryBinding SitesCyclophosphamideCysteineDrug MonitoringHumansMechlorethamineMelphalanNitrogen Mustard CompoundsProtein BindingSerum AlbuminMass spectrometryMatrix-Assisted Laser Desorption-IonizationBrassicaceaeChlorambucil, 305-03-3Cyclophosphamide, 50-18-0Cysteine, 52-90-4Mechlorethamine, 51-75-2Melphalan, 148-82-3Nitrogen Mustard CompoundsNornitrogen mustard, 334-22-5Serum albumin
TNO Identifier
236511
Repository link
https://resolver.tno.nl/uuid:f0047f8e-2256-4bb1-aff3-9f70f9981d14
ISSN
0340-5761
Source
Archives of Toxicology, 76(2), pp. 83-88.
Pages
83-88
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