ArticleJournal of peptide science : an official publication of the European Peptide Society2026
An Effective Method for Isolating Ergothioneine Analogues for Use in Peptide Synthesis: 2-Thiohistidine and Fmoc-2-Thiohistidine.
Article in Journal of peptide science : an official publication of the European Peptide Society, 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
5 authors.
Funding
Abstract
Here, we report on an improved synthesis of the novel amino acid 2-thiohistidine and its Fmoc-derivative through the addition of sodium chloride to the isolation steps of each synthetic procedure. These compounds must be synthesized in either water or a mixture of water/organic solvent and have proven difficult to isolate by traditional methods. We serendipitously discovered that the addition of sodium chloride caused each compound to precipitate from the solution during the workup. Since 2-thiohistidine is the amino acid analogue of the natural product ergothioneine, we hypothesize that sodium cations mimic the binding of other biologically relevant metal cations to the thioimidazole moiety. Ergothioneine is known to bind Cu
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.