ArticleJournal of the American Society for Mass Spectrometry2026
Depsipeptide Analogues of Gly-Ala-Gly: Proton Localization and Effects on Collision-Induced Dissociation.
Article in Journal of the American Society for Mass Spectrometry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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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.
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Who cites it
1 citing paper in PubMed.
- Serine Octamer Substitution Reactions With α-Hydroxy Acids.Rapid communications in mass spectrometry : RCM · 2026Article
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Depsipeptides are peptides that contain both amino acid and hydroxy acid residues. In this study, we sought to investigate how terminal hydroxyl groups and/or backbone ester linkages from hydroxy acid residues in depsipeptides affected collision-induced dissociation (CID). The canonical tripeptide glycine-alanine-glycine (GAG) was compared to all three of its depsipeptide analogues: glycolic acid-AG (gAG), G-lactic acid-G (GaG), and GA-glycolic acid (GAg). Experimental data was supported by density functional theory (DFT) calculations to gain insight into which sites on the molecules have sufficient proton affinity (PA) to localize the proton and the resulting charge-directed fragmentation processes.
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Registered trials
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