The Rhodococcus sp cocaine esterase:: A bacterial candidate for novel pharmacokinetic-based therapies for cocaine abuse

被引:6
作者
Ascenzi, P
Clementi, E
Polticelli, F
机构
[1] Univ Roma Tre, Dipartimento Biol, I-00146 Rome, Italy
[2] Univ Roma Tre, Interdepartmental Lab Electron Microscopy, I-00146 Rome, Italy
[3] DIBIT H San Raffaele Sci Inst, I-20132 Milan, Italy
[4] E Medea Sci Inst, I-23842 Bosisio Parini, Italy
[5] Univ Calabria, Dept Pharmacobiol, I-87036 Arcavacata Di Rende, Italy
关键词
Rhodococcus sp esterase; human plasma butyrylcholinesterase; human liver carboxylesterase-1; human liver carboxylesterase-2; cocaine binding antibodies; cocaine binding catalytic antibodies; cocaine metabolism;
D O I
10.1080/1521654031000138541
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Cocaine is a powerful central nervous stimulant and among the most abused of drugs. Despite decades of efforts, however, no effective pharmacological treatments are available against cocaine addiction or toxic effects. Classical receptor-antagonist therapeutic approaches have not yielded significant effects, although cocaine targets are well known, thus fostering development of alternative therapeutic strategies. Recent evidence indicates that a sensible approach for treatment of cocaine abuse could be to interfere with cocaine pharmacokinetics, i.e. by preventing the drug from reaching the receptors responsible for its biological effects. Administration of cocaine binding antibodies as well as catalytic antibodies and enzymes that hydrolyze cocaine represent potential alternative therapeutic approach(es). The discovery of the cocaine esterase from the strain MB1 of the bacterium Rhodococcus sp. (cocE) could be a major breakthrough in this field; cocE hydrolyzes cocaine faster than any known cocaine esterase and catalytic antibody.
引用
收藏
页码:397 / 402
页数:6
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