A new linker for glucuronylated anticancer prodrugs.
The synthesis, enzymatic hydrolysis and self decomposition of model glucuronylated prodrugs, incorporating a new linker with different aryl substituents, have been studied. Determination of kinetic parameters (V(max), K(m) and t(1/2)) showed the important role of aromatic substitution in enzymatic recognition and linker decomposition.
Rivault
Freddy
F
UMR 6514, Laboratoire de Synthèse et Réactivité des Substances Naturelles, Université de Poitiers, 40 avenue du Recteur Pineau, 86022 Poitiers, France.
Tranoy-Opalinski
Isabelle
I
Gesson
Jean-Pierre
JP
D000438:Alcohols / Q000737:chemistry; D002219:Carbamates / Q000138:chemical synthesis / Q000737:chemistry; D004354:Drug Screening Assays, Antitumor; D004926:Escherichia coli; D000078328:Felbamate; D005965:Glucuronates / Q000737:chemistry*; D005966:Glucuronidase / Q000037:antagonists & inhibitors / Q000378:metabolism; D006868:Hydrolysis / Q000187:drug effects; D007700:Kinetics; D015394:Molecular Structure; D048448:Phenylcarbamates; D011355:Prodrugs / Q000138:chemical synthesis / Q000737:chemistry* / Q000494:pharmacology; D011409:Propylene Glycols / Q000737:chemistry / Q000378:metabolism
D000438:Alcohols; D002219:Carbamates; D005965:Glucuronates; D048448:Phenylcarbamates; D011355:Prodrugs; D011409:Propylene Glycols; D005966:Glucuronidase; D000078328:Felbamate