ArticleChemico-biological interactions2019
Development of a long-acting Fc-fused cocaine hydrolase with improved yield of protein expression.
Article in Chemico-biological interactions, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 22 citations in OpenAlex.
- A cocaine hydrolase engineered from human butyrylcholinesterase as a medical countermeasure for aldicarb poisoning.Chemico-biological interactions · 2025Article
- Treatment of acute organophosphate poisoning by using a cocaine hydrolase engineered from human butyrylcholinesterase.Chemico-biological interactions · 2025Article
- Structural Homology Fails to Predict Secretion Efficiency inInternational journal of molecular sciences · 2025Article
- In vitro and in vivo stability of a highly efficient long-acting cocaine hydrolase.Scientific reports · 2024Article
- Long-lasting blocking of interoceptive effects of cocaine by a highly efficient cocaine hydrolase in rats.Scientific reports · 2024Article
- Catalytic activities of a highly efficient cocaine hydrolase for hydrolysis of biologically active cocaine metabolites norcocaine and benzoylecgonine.Scientific reports · 2023Article
- Gender differences in cocaine-induced hyperactivity and dopamine transporter trafficking to the plasma membrane.Addiction biology · 2022Article
- Recovery of dopaminergic system after cocaine exposure and impact of a long-acting cocaine hydrolase.Addiction biology · 2022Article
- Effects of alcohol on metabolism and toxicity of cocaine in rats.Toxicology reports · 2022Article
- Cocaine hydrolase blocks cocaine-induced dopamine transporter trafficking to the plasma membrane.Addiction biology · 2022Article
- Systematic Structure-Based Virtual Screening Approach to Antibody Selection and Design of a Humanized Antibody against Multiple Addictive Opioids without Affecting Treatment Agents Naloxone and Naltrexone.ACS chemical neuroscience · 2021Article
- Clinical potential of a rationally engineered enzyme for treatment of cocaine dependence: Long-lasting blocking of the psychostimulant, discriminative stimulus, and reinforcing effects of cocaine.Neuropharmacology · 2020Article
- Structure-Based Design and Discovery of a Long-Acting Cocaine Hydrolase Mutant with Improved Binding Affinity to Neonatal Fc Receptor for Treatment of Cocaine Abuse.The AAPS journal · 2020Article
- Reengineering of Albumin-Fused Cocaine Hydrolase CocH1 (TV-1380) to Prolong Its Biological Half-Life.The AAPS journal · 2019Article
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
Human butyrylcholinesterase (BChE) is known as a safe and effective protein for detoxification of organophosphorus (OP) nerve agents. Its rationally designed mutants with considerably improved catalytic activity against cocaine, known as cocaine hydrolases (CocHs), are recognized as the most promising drug candidates for the treatment of cocaine abuse. However, it is a grand challenge to efficiently produce active recombinant BChE and CocHs with a sufficiently long biological half-life. In the present study, starting from a promising CocH, known as CocH3 (i.e. A199S/F227A/S287G/A328W/Y332G mutant of human BChE), which has a ~2000-fold improved catalytic activity against cocaine compared to wild-type BChE, we designed an N-terminal fusion protein, Fc(M3)-(PAPAP)
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