ArticleChembiochem : a European journal of chemical biology2021
Effect of Methionine Sulfoxide on the Synthesis and Purification of Aggregation-Prone Peptides.
Article in Chembiochem : a European journal of chemical biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 13 citations in OpenAlex.
- Peptide Thioester and Triazole Derivatives Through On-Resin Dual-Modification of Peptide Thiosulfonates.Angewandte Chemie (International ed. in English) · 2026Article
- Chemical Synthesis of Crustacean Insulin-Like Peptide Using a Novel Method to Prevent Methionine Oxidation During Solid Phase Peptide Synthesis.Journal of peptide science : an official publication of the European Peptide Society · 2025Article
- Chemical Protein Engineering: Backbone Cyclization Rescues Folding of a 183-Residue Truncated Domain of Malaria Parasite Protein PfAMA1.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- The emergence and loss of cyclic peptides inProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Thanatin and vinyl sulfide analogues as narrow spectrum antimicrobial peptides that synergise with polymyxin B.Frontiers in pharmacology · 2024Article
- The CSY-protecting group in the microwave-assisted synthesis of aggregation-prone peptides.RSC chemical biology · 2022Article
- Development of an Off-Grid Solar-Powered Autonomous Chemical Mini-Plant for Producing Fine Chemicals.ChemSusChem · 2021Article
- Effect of Methionine Sulfoxide on the Synthesis and Purification of Aggregation-Prone Peptides.Chembiochem : a European journal of chemical biology · 2021Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
A two-step synthesis for methionine-containing hydrophobic and/or aggregation-prone peptides is presented that takes advantage of the reversibility of methionine oxidation. The use of polar methionine sulfoxide as a building block in solid-phase peptide synthesis improves the synthesis quality and yields the crude peptide, with significantly improved solubility compared to the reduced species. This facilitates the otherwise often laborious peptide purification by high-performance liquid chromatography. The subsequent reduction proceeds quantitatively. This approach has been optimised with the methionine-rich Tar-DNA-binding protein 43 (307-347), but is also more generally applicable, as demonstrated by the syntheses of human calcitonin and two aggregation-prone peptides from the human prion protein.
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Registered trials
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