Abstract：
:Butyrylcholinesterase (BChE, EC 3.1.1.8) is important in human cocaine metabolism despite its limited ability to hydrolyze this drug. Efforts to improve the catalytic efficiency of this enzyme have led to a quadruple mutant cocaine hydrolase, "CocH", that in animal models of addiction appears promising for treatment of overdose and relapse. We incorporated the CocH mutations into a BChE-albumin fusion protein, "Albu-CocH", and evaluated the pharmacokinetics of the enzyme after i.v. injection in rats. As assessed from the time course of cocaine hydrolyzing activity in plasma, Albu-CocH redistributed into extracellular fluid (16% of estimated total body water) with a t(1/2) of 0.66h and it underwent elimination with a t(1/2) of 8h. These results indicate that the enzyme has ample stability for short-term applications and may be suitable for longer-term treatment as well. Present data also confirm the markedly enhanced power of Albu-CocH for cocaine hydrolysis and they support the view that Albu-CocH might prove valuable in treating phenomena associated with cocaine abuse.
journal_name
Chem Biol Interactjournal_title
Chemico-biological interactionsauthors
Gao Y,LaFleur D,Shah R,Zhao Q,Singh M,Brimijoin Sdoi
10.1016/j.cbi.2008.04.024subject
Has Abstractpub_date
2008-09-25 00:00:00pages
83-7issue
1-3eissn
0009-2797issn
1872-7786pii
S0009-2797(08)00211-1journal_volume
175pub_type
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