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 journalArticle

11 Citations (Scopus)
5 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 languageEnglish
Pages (from-to)10998-11004
Number of pages7
JournalChemistry : a European Journal
Volume22
Issue number31
Early online date4 Jul 2016
DOIs
Publication statusPublished - 25 Jul 2016

Fingerprint

Fluorination
Peptides
Cysteine
Sulfur
Integrins
Cells
Substrates
fluorinase
arginyl-glycyl-aspartic acid

Keywords

  • 18F Labelling
  • RGD Peptide
  • chemical biology
  • Barbas linker
  • bioconjugation

Cite this

Last-step enzymatic [18F]-fluorination of cysteine-tethered RGD peptides using modified Barbas linkers. / Zhang, Qingzhi; Dall'Angelo, Sergio; Fleming, Ian N.; Schweiger, Lutz F.; Zanda, Matteo; O'Hagan, David.

In: Chemistry : a European Journal, Vol. 22, No. 31, 25.07.2016, p. 10998-11004.

Research output: Contribution to journalArticle

@article{1cd84492d7e74e05b5d24f47ee58ffaf,
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",
year = "2016",
month = "7",
day = "25",
doi = "10.1002/chem.201601361",
language = "English",
volume = "22",
pages = "10998--11004",
journal = "Chemistry : a European Journal",
issn = "0947-6539",
publisher = "WILEY-V C H VERLAG GMBH",
number = "31",

}

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

VL - 22

SP - 10998

EP - 11004

JO - Chemistry : a European Journal

JF - Chemistry : a European Journal

SN - 0947-6539

IS - 31

ER -