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磷酸肽的铀酰光裂解产生截短的C端酰胺化肽产物。

Uranyl Photocleavage of Phosphopeptides Yields Truncated C-Terminally Amidated Peptide Products.

作者信息

Elnegaard Rasmus L B, Møllegaard Niels Erik, Zhang Qiang, Kjeldsen Frank, Jørgensen Thomas J D

机构信息

Department of Biochemistry and Molecular Biology, University of Southern Denmark, Campusvej 55, 5230, Odense M, Denmark.

Department of Cellular and Molecular Medicine, University of Copenhagen, Blegdamsvej 3B, 2200, Copenhagen N, Denmark.

出版信息

Chembiochem. 2017 Jun 19;18(12):1117-1122. doi: 10.1002/cbic.201700103. Epub 2017 May 23.

Abstract

The uranyl ion (UO ) 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.

摘要

铀酰离子(UO )能以高亲和力结合磷酸肽,并且在紫外光照射下,它可以切割肽主链。在本研究中,利用高精度串联质谱和酶促测定来表征四磷酸化β-酪蛋白模型肽的铀酰光切割反应产生的光切割产物。我们表明,铀酰催化反应的主要光切割产物是C端酰胺化的。这可能会引起制药行业的极大兴趣,因为高效的肽酰胺化反应是绿色药物化学中的首要挑战之一。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c3db/5488209/14a4c6f06091/CBIC-18-1117-g001.jpg

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