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

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Uranyl Photocleavage of Phosphopeptides Yields Truncated C-Terminally Amidated Peptide Products. / Elnegaard, Rasmus L B; Møllegaard, Niels Erik; Zhang, Qiang; Kjeldsen, Frank; Jørgensen, Thomas J D.

In: ChemBioChem, Vol. 18, No. 12, 19.06.2017, p. 1117-1122.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Elnegaard, RLB, Møllegaard, NE, Zhang, Q, Kjeldsen, F & Jørgensen, TJD 2017, 'Uranyl Photocleavage of Phosphopeptides Yields Truncated C-Terminally Amidated Peptide Products', ChemBioChem, vol. 18, no. 12, pp. 1117-1122. https://doi.org/10.1002/cbic.201700103

APA

Elnegaard, R. L. B., Møllegaard, N. E., Zhang, Q., Kjeldsen, F., & Jørgensen, T. J. D. (2017). Uranyl Photocleavage of Phosphopeptides Yields Truncated C-Terminally Amidated Peptide Products. ChemBioChem, 18(12), 1117-1122. https://doi.org/10.1002/cbic.201700103

Vancouver

Elnegaard RLB, Møllegaard NE, Zhang Q, Kjeldsen F, Jørgensen TJD. Uranyl Photocleavage of Phosphopeptides Yields Truncated C-Terminally Amidated Peptide Products. ChemBioChem. 2017 Jun 19;18(12):1117-1122. https://doi.org/10.1002/cbic.201700103

Author

Elnegaard, Rasmus L B ; Møllegaard, Niels Erik ; Zhang, Qiang ; Kjeldsen, Frank ; Jørgensen, Thomas J D. / Uranyl Photocleavage of Phosphopeptides Yields Truncated C-Terminally Amidated Peptide Products. In: ChemBioChem. 2017 ; Vol. 18, No. 12. pp. 1117-1122.

Bibtex

@article{8fe9037de0d044928ea47c4177d6d367,
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,
day = "19",
doi = "10.1002/cbic.201700103",
language = "English",
volume = "18",
pages = "1117--1122",
journal = "ChemBioChem",
issn = "1439-4227",
publisher = "Wiley - V C H Verlag GmbH & Co. KGaA",
number = "12",

}

RIS

TY - JOUR

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

N1 - © 2017 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA.

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

VL - 18

SP - 1117

EP - 1122

JO - ChemBioChem

JF - ChemBioChem

SN - 1439-4227

IS - 12

ER -

ID: 181383513