ArticleJournal of peptide science : an official publication of the European Peptide Society2026
Reductive Methylation: An Alternative to Lysine → Arginine Mutagenesis.
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. 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
1 citing paper in PubMed.
- Reductive Methylation: An Alternative to Lysine → Arginine Mutagenesis.Journal of peptide science : an official publication of the European Peptide Society · 2026Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Modification of lysine residues is a common strategy in protein engineering, whether to prevent posttranslational modifications, control bioconjugation, or improve crystallization. The standard genetic approach-replacement with arginine by site-directed mutagenesis-preserves positive charge but alters other physicochemical attributes and cannot address the N-terminal amino group. Here, we characterize reductive methylation as a chemical alternative. This reaction converts every primary amino group to a dimethylamino group rapidly under mild aqueous conditions. Using human ribonuclease 1 and a cytotoxic variant engineered to evade the endogenous ribonuclease inhibitor as model systems, we assess the effects of complete dimethylation on thermostability, enzymatic catalysis, protein-protein interaction, compatibility with bioconjugation, cellular uptake, and intracellular persistence. Dimethylation preserves thermostability and a protein-protein interaction. Enzymatic catalysis, in contrast, is reduced by 10
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