ArticleBioanalysis2025
In-vitro metabolite identification for MEDI7219, an oral GLP-1 analog, using LC-MS/MS with CID and EAD approaches.
Article in Bioanalysis, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed.
- Development and validation of a sensitive HPLC-MS/MS method for the analysis of semaglutide in human plasma.Bioanalysis · 2026Article
- Strategies for overcoming multiple barriers of oral administration of protein and peptide therapeutics.Materials today. Bio · 2026Review
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
aimOral peptide therapeutics typically have short half-lives due to rapid degradation by digestive enzymes. Systematic peptide engineering and formulation optimization led to the development of a clinical candidate MEDI7219, an orally bioavailable glucagon-like peptide 1 (GLP-1) peptide, with greater stability than wild-type GLP-1 or semaglutide:~60% of MEDI7219 remained intact after 2 h in vitro incubation with simulated intestinal fluid. This study further investigates proteolytic stability by elucidating biotransformation products of MEDI7219 using liquid chromatography-mass spectrometry (LC-MS) methods.
methodPeptide metabolism was assessed using in vitro pancreatin assay followed by analysis utilizing liquid chromatography coupled with tandem mass spectrometry (LC-MS/MS) using collision-induced dissociation (CID) and electron-activated dissociation (EAD) approaches.
resultsWe have confidently identified 13 metabolites. Time course profiles of parent and metabolite peaks are consistent with sequential enzymatic cleavage pattern. The 13 metabolites mapped to 8 cleavage sites. Most of these cleavage sites can be explained by the specificity of digestive enzymes,
conclusionThese study results provide further structural details explaining previously published stability data and provide new insights into potential GLP1 proteolytic liabilities for future engineering.
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