Ion mobility MS reveals conformational heterogeneity in ziconotide and linaclotide batches
Cyclic IM-MS detected coexisting conformers and stress-induced structural reorganization that conventional analytical methods missed.
PR
By Priya Raman · Science Reporter
Aug 16 20:00 ETSource: Frontiers in chemistry
The wire
- 01Researchers applied cyclic ion mobility-mass spectrometry with accelerated thermal stress testing to manufacturing batches of ziconotide and linaclotide, finding pronounced conformational heterogeneity even under native conditions.
- 02Disulfide-rich peptide drugs depend on rigid cystine architecture for stability and target specificity, so undetected higher-order variation is a quality-control gap for manufacturers and pharmacists handling these products.
- 03The study covers single batches of two marketed peptides and does not link the observed conformers to potency, immunogenicity or clinical outcomes.
From the source
Read at pubmed.ncbi.nlm.nih.govResolving conformational polymorphism in disulfide-rich peptide drugs
Frontiers in chemistry · 2026 · Zhu S, Ge Y, Huang H et al.
Source URL https://pubmed.ncbi.nlm.nih.gov/42676398/