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

25 Citations (Scopus)

13 Downloads (Pure)

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

UN SDGs

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

SDG 3 Good Health and Well-being

Keywords

18F Labelling
RGD Peptide
chemical biology
Barbas linker
bioconjugation

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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, 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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doi = "10.1002/chem.201601361",

language = "English",

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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 - 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

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

Bibliographical note

UN SDGs

Keywords

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Sergio Dall'Angelo

Ian Fleming

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