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Uranyl Photocleavage of Phosphopeptides Yields Truncated C‐Terminally Amidated Peptide Products

The uranyl ion (UO(2) (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 photo...

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Detalles Bibliográficos
Autores principales: Elnegaard, Rasmus L. B., Møllegaard, Niels Erik, Zhang, Qiang, Kjeldsen, Frank, Jørgensen, Thomas J. D.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5488209/
https://www.ncbi.nlm.nih.gov/pubmed/28425166
http://dx.doi.org/10.1002/cbic.201700103
Descripción
Sumario:The uranyl ion (UO(2) (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.