ArticleACS pharmacology & translational science2026
Discovery, Structural Characterization, and Preclinical Evaluation of Monoclonal Antibodies against Xylazine Poisoning.
Article in ACS pharmacology & translational science, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
14 authors.
Funding
Abstract
Xylazine is a nonopioid sedative that has emerged as a major adulterant in the illicit drug supply, contributing to rising fatal overdoses across the United States. Xylazine toxicity is not reversed by naloxone, and there are no current FDA-approved therapeutics to counteract its effects in humans. To address this issue, we developed and characterized monoclonal antibodies (mAbs) capable of sequestering xylazine to prevent or treat acute toxicity. By immunizing mice with conjugated haptens targeting distinct epitopes of the xylazine molecule, we generated two lead candidates, Xy1001 and Xy3001. Comparative kinetic analysis revealed that Xy3001 showed a subnanomolar affinity and was selected for structural characterization. X-ray crystallography of the Xy3001-xylazine complex revealed the structural basis for this affinity, showing the binding of xylazine in a deep pocket anchored by hydrogen bonding. Humanization of Xy3001 resulted in a minor reduction in affinity but demonstrated improved biophysical stability and high specificity with no significant cross-reactivity to off-target opioids or stimulants. In a murine model of toxicity, prophylactic administration of both lead candidates significantly attenuated xylazine-induced antinociception, with Xy3001 demonstrating additional mitigation of respiratory depression and bradycardia. Pharmacokinetic analysis demonstrated that mAb treatment limited xylazine entry into the brain. This study validates peripheral sequestration against xylazine as a therapeutic strategy with future efforts aimed at optimization of these lead candidates to increase translational potential.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.