ArticleProceedings of the National Academy of Sciences of the United States of America2016
Long-acting cocaine hydrolase for addiction therapy.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers, 1 of them a synthesis that pooled it.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
37 citing papers in PubMed, 1 synthesis or guideline pooled it, 62 citations in OpenAlex.
- Clinical data mining reveals analgesic effects of lapatinib in cancer patients.Scientific reports · 2021Pooled it
- Observation of aldicarb hydrolysis by a cocaine hydrolase.Bioscience reports · 2026Article
- 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
- 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
- Gender differences in cocaine-induced hyperactivity and dopamine transporter trafficking to the plasma membrane.Addiction biology · 2022Article
- Immunotherapies for the Treatment of Drug Addiction.Vaccines · 2022Review
- Recovery of dopaminergic system after cocaine exposure and impact of a long-acting cocaine hydrolase.Addiction biology · 2022Article
- Cocaine hydrolase blocks cocaine-induced dopamine transporter trafficking to the plasma membrane.Addiction biology · 2022Article
- Understanding the genetics and neurobiological pathways behind addiction (Review).Experimental and therapeutic medicine · 2021Review
- 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
- Cebranopadol reduces cocaine self-administration in male rats: Dose, treatment and safety consideration.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
- Catalytic activities of cocaine hydrolases against the most toxic cocaine metabolite norcocaethylene.Organic & biomolecular chemistry · 2020Article
- PEGylation but Not Fc-Fusion Improves in Vivo Residence Time of a Thermostable Mutant of Bacterial Cocaine Esterase.Bioconjugate chemistry · 2019Article
- Development of a novel prostate apoptosis response-4 (Par-4) protein entity with an extended duration of action for therapeutic treatment of cancer.Protein engineering, design & selection : PEDS · 2019Article
- Reengineering of Albumin-Fused Cocaine Hydrolase CocH1 (TV-1380) to Prolong Its Biological Half-Life.The AAPS journal · 2019Article
- Development of a long-acting Fc-fused cocaine hydrolase with improved yield of protein expression.Chemico-biological interactions · 2019Article
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7 authors at 1 institution in 1 country.
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Abstract
Cocaine abuse is a world-wide public health and social problem without a US Food and Drug Administration-approved medication. An ideal anticocaine medication would accelerate cocaine metabolism, producing biologically inactive metabolites by administration of an efficient cocaine-specific exogenous enzyme. Our recent studies have led to the discovery of the desirable, highly efficient cocaine hydrolases (CocHs) that can efficiently detoxify and inactivate cocaine without affecting normal functions of the CNS. Preclinical and clinical data have demonstrated that these CocHs are safe for use in humans and are effective for accelerating cocaine metabolism. However, the actual therapeutic use of a CocH in cocaine addiction treatment is limited by its short biological half-life (e.g., 8 h or shorter in rats). Here we demonstrate a novel CocH form, a catalytic antibody analog, which is a fragment crystallizable (Fc)-fused CocH dimer (CocH-Fc) constructed by using CocH to replace the Fab region of human IgG1. The CocH-Fc not only has a high catalytic efficiency against cocaine but also, like an antibody, has a considerably longer biological half-life (e.g., ∼107 h in rats). A single dose of CocH-Fc was able to accelerate cocaine metabolism in rats even after 20 d and thus block cocaine-induced hyperactivity and toxicity for a long period. Given the general observation that the biological half-life of a protein drug is significantly longer in humans than in rodents, the CocH-Fc reported in this study could allow dosing once every 2-4 wk, or longer, for treatment of cocaine addiction in humans.
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