Uranyl Photocleavage of Phosphopeptides Yields Truncated C-Terminally Amidated Peptide Products
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- Uranyl Photocleavage of Phosphopeptides Yields Truncated C-Terminally Amidated Peptide Products
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The uranyl ion (UO2(2+) ) binds phosphopeptides with high affinity, and when irradiated with UV-light, it can cleave the peptide backbone. In this study, high-accuracy tandem mass spectrometry and enzymatic assays were used to characterise the photocleavage products resulting from the uranyl photocleavage reaction of a tetraphosphorylated β-casein model peptide. We show that the primary photocleavage products of the uranyl-catalysed reaction are C-terminally amidated. This could be of great interest to the pharmaceutical industry, as efficient peptide amidation reactions are one of the top challenges in green pharmaceutical chemistry.
Original language | English |
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Journal | ChemBioChem |
Volume | 18 |
Issue number | 12 |
Pages (from-to) | 1117-1122 |
Number of pages | 6 |
ISSN | 1439-4227 |
DOIs | |
Publication status | Published - 19 Jun 2017 |
- Amides, Amino Acid Sequence, Carboxypeptidases, Caseins, Cations, Divalent, Enzyme Assays, Green Chemistry Technology, Phosphopeptides, Photolysis, Protein Binding, Tandem Mass Spectrometry, Ultraviolet Rays, Uranium Compounds, Journal Article
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