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

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

doi:10.1002/cbic.201700103

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

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

5 Citations (Scopus)

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Abstract

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
Journal	ChemBioChem
Volume	18
Issue number	12
Pages (from-to)	1117-1122
Number of pages	6
ISSN	1439-4227
DOIs	https://doi.org/10.1002/cbic.201700103
Publication status	Published - 19 Jun 2017

Keywords

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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Uranyl Photocleavage of Phosphopeptides Yields Truncated C-Terminally Amidated Peptide ProductsFinal published version, 1.06 MBLicence: CC BY-NC-ND

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title = "Uranyl Photocleavage of Phosphopeptides Yields Truncated C-Terminally Amidated Peptide Products",

abstract = "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.",

keywords = "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",

author = "Elnegaard, {Rasmus L B} and M{\o}llegaard, {Niels Erik} and Qiang Zhang and Frank Kjeldsen and J{\o}rgensen, {Thomas J D}",

note = "{\textcopyright} 2017 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA.",

year = "2017",

month = jun,

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doi = "10.1002/cbic.201700103",

language = "English",

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T1 - Uranyl Photocleavage of Phosphopeptides Yields Truncated C-Terminally Amidated Peptide Products

AU - Elnegaard, Rasmus L B

AU - Møllegaard, Niels Erik

AU - Zhang, Qiang

AU - Kjeldsen, Frank

AU - Jørgensen, Thomas J D

PY - 2017/6/19

Y1 - 2017/6/19

N2 - 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.

AB - 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.

KW - Amides

KW - Amino Acid Sequence

KW - Carboxypeptidases

KW - Caseins

KW - Cations, Divalent

KW - Enzyme Assays

KW - Green Chemistry Technology

KW - Phosphopeptides

KW - Photolysis

KW - Protein Binding

KW - Tandem Mass Spectrometry

KW - Ultraviolet Rays

KW - Uranium Compounds

KW - Journal Article

U2 - 10.1002/cbic.201700103

DO - 10.1002/cbic.201700103

M3 - Journal article

C2 - 28425166

SN - 1439-4227

VL - 18

SP - 1117

EP - 1122

JO - ChemBioChem

JF - ChemBioChem

IS - 12

ER -

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

Abstract

Keywords

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