Last-step enzymatic [18F]-fluorination of cysteine-tethered RGD peptides using modified Barbas linkers

Qingzhi Zhang; Sergio Dall'Angelo; Ian N. Fleming; Lutz F. Schweiger; Matteo Zanda; David O'Hagan

doi:10.1002/chem.201601361

Last-step enzymatic [18F]-fluorination of cysteine-tethered RGD peptides using modified Barbas linkers

Qingzhi Zhang, Sergio Dall'Angelo, Ian N. Fleming, Lutz F. Schweiger, Matteo Zanda, David O'Hagan

University of St Andrews

Research output: Contribution to journal › Article › peer-review

22 Citations (Scopus)

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Abstract

We report a last-step fluorinase catalyzed [18F]-fluorination of a cysteine-containing RGD peptide. The peptide was attached through sulfur to a modified and more hydrophilic variant of the recently disclosed Barbas linker which was itself linked to a chloroadenosine moiety via a PEGylated chain. The fluorinase was able to use this construct as a substrate for a transhalogenation reaction to generate [18F]-radiolabelled RGD peptides, which retained high affinity to cancer cell relevant αvβ3 integrins

Original language	English
Pages (from-to)	10998-11004
Number of pages	7
Journal	Chemistry : a European Journal
Volume	22
Issue number	31
Early online date	4 Jul 2016
DOIs	https://doi.org/10.1002/chem.201601361
Publication status	Published - 25 Jul 2016

Bibliographical note

Acknowledgements
We thank the Engineering and Physical Sciences Research Council, UK, for a research grant.

Funded by
Engineering and Physical Sciences Research Council, UK

Keywords

18F Labelling
RGD Peptide
chemical biology
Barbas linker
bioconjugation

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1002/chem.201601361Licence: Unspecified

Accepted Manuscript
This is the peer reviewed version of the following article: Q. Zhang, S. Dall'Angelo, I. N. Fleming, L. F. Schweiger, M. Zanda, D. O'Hagan, 'Last-Step Enzymatic [18F]-Fluorination of Cysteine-Tethered RGD Peptides Using Modified Barbas Linkers' Chemistry: A European Journal. 2016, 22(31), pp: 10998–11004, which has been published in final form at http://dx.doi.org/10.1002/chem.201601361. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Self-Archiving.
Accepted author manuscript, 346 KBLicence: Unspecified

Sergio Dall'Angelo
Person: Academic Related - Research
Ian Fleming
- School of Medicine, Medical Sciences & Nutrition, Medical Education - Senior Lecturer (Scholarship)
- School of Medicine, Medical Sciences & Nutrition, Aberdeen Biomedical Imaging Centre
Person: Academic Related - Scholarship

Cite this

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title = "Last-step enzymatic [18F]-fluorination of cysteine-tethered RGD peptides using modified Barbas linkers",

abstract = "We report a last-step fluorinase catalyzed [18F]-fluorination of a cysteine-containing RGD peptide. The peptide was attached through sulfur to a modified and more hydrophilic variant of the recently disclosed Barbas linker which was itself linked to a chloroadenosine moiety via a PEGylated chain. The fluorinase was able to use this construct as a substrate for a transhalogenation reaction to generate [18F]-radiolabelled RGD peptides, which retained high affinity to cancer cell relevant αvβ3 integrins",

keywords = "18F Labelling , RGD Peptide , chemical biology, Barbas linker, bioconjugation",

author = "Qingzhi Zhang and Sergio Dall'Angelo and Fleming, {Ian N.} and Schweiger, {Lutz F.} and Matteo Zanda and David O'Hagan",

note = "Acknowledgements We thank the Engineering and Physical Sciences Research Council, UK, for a research grant. Funded by Engineering and Physical Sciences Research Council, UK",

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language = "English",

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T1 - Last-step enzymatic [18F]-fluorination of cysteine-tethered RGD peptides using modified Barbas linkers

AU - Zhang, Qingzhi

AU - Dall'Angelo, Sergio

AU - Fleming, Ian N.

AU - Schweiger, Lutz F.

AU - Zanda, Matteo

AU - O'Hagan, David

N1 - Acknowledgements We thank the Engineering and Physical Sciences Research Council, UK, for a research grant. Funded by Engineering and Physical Sciences Research Council, UK

PY - 2016/7/25

Y1 - 2016/7/25

N2 - We report a last-step fluorinase catalyzed [18F]-fluorination of a cysteine-containing RGD peptide. The peptide was attached through sulfur to a modified and more hydrophilic variant of the recently disclosed Barbas linker which was itself linked to a chloroadenosine moiety via a PEGylated chain. The fluorinase was able to use this construct as a substrate for a transhalogenation reaction to generate [18F]-radiolabelled RGD peptides, which retained high affinity to cancer cell relevant αvβ3 integrins

AB - We report a last-step fluorinase catalyzed [18F]-fluorination of a cysteine-containing RGD peptide. The peptide was attached through sulfur to a modified and more hydrophilic variant of the recently disclosed Barbas linker which was itself linked to a chloroadenosine moiety via a PEGylated chain. The fluorinase was able to use this construct as a substrate for a transhalogenation reaction to generate [18F]-radiolabelled RGD peptides, which retained high affinity to cancer cell relevant αvβ3 integrins

KW - 18F Labelling

KW - RGD Peptide

KW - chemical biology

KW - Barbas linker

KW - bioconjugation

U2 - 10.1002/chem.201601361

DO - 10.1002/chem.201601361

M3 - Article

SN - 0947-6539

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SP - 10998

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JO - Chemistry : a European Journal

JF - Chemistry : a European Journal

IS - 31

ER -

Last-step enzymatic [18F]-fluorination of cysteine-tethered RGD peptides using modified Barbas linkers

Abstract

Bibliographical note

Keywords

UN SDGs

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Sergio Dall'Angelo

Ian Fleming

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