ArticleProtein science : a publication of the Protein Society2009
Crystal structures of a therapeutic single chain antibody in complex with two drugs of abuse-Methamphetamine and 3,4-methylenedioxymethamphetamine.
Article in Protein science : a publication of the Protein Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 23 citations in OpenAlex.
- Site-Specific PEGylation of Anti-Mesothelin Recombinant Immunotoxins Increases Half-life and Antitumor Activity.Molecular cancer therapeutics · 2020Article
- Chronic treatment of (+)-methamphetamine-induced locomotor effects in rats using one or a combination of two high affinity anti-methamphetamine monoclonal antibodies.Human vaccines & immunotherapeutics · 2016Article
- Protective effect of pentoxifylline on male Wistar rat testicular germ cell apoptosis induced by 3,4-methylenedioxymeth amphetamine.Iranian journal of basic medical sciences · 2016Article
- Affinity improvement of a therapeutic antibody to methamphetamine and amphetamine through structure-based antibody engineering.Scientific reports · 2014Article
- Customizing monoclonal antibodies for the treatment of methamphetamine abuse: current and future applications.Advances in pharmacology (San Diego, Calif.) · 2014Review
- Structural characterization of a therapeutic anti-methamphetamine antibody fragment: oligomerization and binding of active metabolites.PloS one · 2013Article
- Therapeutic anti-methamphetamine antibody fragment-nanoparticle conjugates: synthesis and in vitro characterization.Bioconjugate chemistry · 2012Article
- Pharmacokinetic strategies for treatment of drug overdose and addiction.Future medicinal chemistry · 2012Review
- Insights into scFv:drug binding using the molecular dynamics simulation and free energy calculation.Journal of molecular modeling · 2011Article
- In silico experiments of single-chain antibody fragment against drugs of abuse.Biophysical chemistry · 2010Article
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Authors and funding
4 authors at 1 institution in 1 country.
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Abstract
Methamphetamine (METH) is a major drug threat in the United States and worldwide. Monoclonal antibody (mAb) therapy for treating METH abuse is showing exciting promise and the understanding of how mAb structure relates to function will be essential for future development of these important therapies. We have determined crystal structures of a high affinity anti-(+)-METH therapeutic single chain antibody fragment (scFv6H4, K(D)= 10 nM) derived from one of our candidate mAb in complex with METH and the (+) stereoisomer of another abused drug, 3,4-methylenedioxymethamphetamine (MDMA), known by the street name "ecstasy." The crystal structures revealed that scFv6H4 binds to METH and MDMA in a deep pocket that almost completely encases the drugs mostly through aromatic interactions. In addition, the cationic nitrogen of METH and MDMA forms a salt bridge with the carboxylate group of a glutamic acid residue and a hydrogen bond with a histidine side chain. Interestingly, there are two water molecules in the binding pocket and one of them is positioned for a C--H...O interaction with the aromatic ring of METH. These first crystal structures of a high affinity therapeutic antibody fragment against METH and MDMA (resolution = 1.9 A, and 2.4 A, respectively) provide a structural basis for designing the next generation of higher affinity antibodies and also for carrying out rational humanization.
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