Abstract
A large number of bioactive peptides are cyclized through a disulfide bridge. This structural feature is very important for both bioactivity and stability. The oxidation of cysteine side chains is challenging not only to avoid intermolecular reaction leading to oligomers and oxidation of other residues but also to remove solvents and oxidant such as dimethyl sulfoxide. Supported reagents advantageously simplify the work-up of such disulfide bond formation, but may lead to a significant decrease in yield of the oxidized product. In this study, two resins working through different mechanisms were evaluated: Clear-Ox, a supported version of Ellman’s reagent and Oxyfold, consisting in a series of oxidized methionine residues. The choice of the supported reagent is discussed on the light of reaction speed, side-products formation and yield considerations.
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L. Ronga and P. Verdié are equal contributors to the study.
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Ronga, L., Verdié, P., Sanchez, P. et al. Supported oligomethionine sulfoxide and Ellman’s reagent for cysteine bridges formation. Amino Acids 44, 733–742 (2013). https://doi.org/10.1007/s00726-012-1397-5
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DOI: https://doi.org/10.1007/s00726-012-1397-5