ArticleJournal of peptide science : an official publication of the European Peptide Society2025
DiPTH-Cystine and PTH-Cysteine in Disulfide Bond Analysis Using Automated Edman Degradation.
Article in Journal of peptide science : an official publication of the European Peptide Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
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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.
- DiPTH-Cystine and PTH-Cysteine in Disulfide Bond Analysis Using Automated Edman Degradation.Journal of peptide science : an official publication of the European Peptide Society · 2025Article
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Authors and funding
4 authors.
Funding
Abstract
The annotation of disulfide bridges in peptides and proteins can be an elaborate process and requires careful revision of multiple data sets to avoid wrong assignment in the structural analysis. Herein, we provide additional support to elucidate the cysteine connectivity by re-implementation of Edman sequencing for the analysis of this specific structural feature. By synthesizing diPTH-cystine and PTH-cysteine for comparison, we were able to identify the respective derivative during Edman sequencing when a disulfide bond is detected in a peptide. Application of Edman sequencing to selected peptides with two or three disulfide bridges provides further insight into the differentiation of cysteines that form a disulfide bridge for both half-cystines in the same cycle and in separated cycles. A combined approach for the implementation of automated Edman sequencing in the process of disulfide bond assignment is described to alleviate structural elucidation in the future analysis of cysteine-rich peptides and proteins.
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Registered trials
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