Premium
Uranyl Photocleavage of Phosphopeptides Yields Truncated C‐Terminally Amidated Peptide Products
Author(s) -
Elnegaard Rasmus L. B.,
Møllegaard Niels Erik,
Zhang Qiang,
Kjeldsen Frank,
Jørgensen Thomas J. D.
Publication year - 2017
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201700103
Subject(s) - uranyl , chemistry , cleave , peptide , combinatorial chemistry , mass spectrometry , tandem mass spectrometry , ion , organic chemistry , enzyme , biochemistry , chromatography
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.