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

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

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]-radiolabeled RGD peptides, which retained high affinity to cancer-cell relevant α_vβ₃ integrins.

Original language	English
Pages (from-to)	10998–11004
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

Keywords

18F labeling
Barbas linker
Bioconjugation
Chemical biology
RGD peptide

UN SDGs

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

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10.1002/chem.201601361

May 13th Chem Eur J
© 2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim. This work is made available online in accordance with the publisher’s policies. This is the author created, accepted version manuscript following peer review and may differ slightly from the final published version. The final published version of this work is available at https://dx.doi.org/10.1002/chem.201601361
Accepted author manuscript, 970 KB

Last Step 18F Labelling for PET: 'Last Step' enzymatic [18F]-labelling of peptides for Positron Emission Tomography (PET)
O'Hagan, D. (PI)
EPSRC
28/02/15 → 28/02/18
Project: Standard
Extending fluorinase C-18F-bond: Extending fluorinase [C-18F]-bond biocatalysis for Positron Emission Tomography (PET)
O'Hagan, D. (PI)
EPSRC
1/11/11 → 31/10/14
Project: Standard

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]-radiolabeled RGD peptides, which retained high affinity to cancer-cell relevant αvβ3 integrins.",

keywords = "18F labeling, Barbas linker, Bioconjugation, Chemical biology, RGD peptide",

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

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

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doi = "10.1002/chem.201601361",

language = "English",

volume = "22",

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journal = "Chemistry - A European Journal",

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TY - JOUR

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

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]-radiolabeled 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]-radiolabeled RGD peptides, which retained high affinity to cancer-cell relevant αvβ3 integrins.

KW - 18F labeling

KW - Barbas linker

KW - Bioconjugation

KW - Chemical biology

KW - RGD peptide

U2 - 10.1002/chem.201601361

DO - 10.1002/chem.201601361

M3 - Article

SN - 1521-3765

VL - 22

SP - 10998

EP - 11004

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

Keywords

UN SDGs

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Projects

Last Step 18F Labelling for PET: 'Last Step' enzymatic [18F]-labelling of peptides for Positron Emission Tomography (PET)

Extending fluorinase C-18F-bond: Extending fluorinase [C-18F]-bond biocatalysis for Positron Emission Tomography (PET)

Cite this

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