Home > Research > Publications & Outputs > Development, characterisation and in vitro eval...

Electronic data

  • terbium dalton V25

    Rights statement: © Royal Society of Chemistry 2020

    Accepted author manuscript, 2.41 MB, PDF document

    Available under license: CC BY-NC: Creative Commons Attribution-NonCommercial 4.0 International License

Links

Text available via DOI:

View graph of relations

Development, characterisation and in vitro evaluation of lanthanide-based FPR2/ALX-targeted imaging probes

Research output: Contribution to Journal/MagazineJournal articlepeer-review

Published

Standard

Development, characterisation and in vitro evaluation of lanthanide-based FPR2/ALX-targeted imaging probes. / Boltersdorf, Tamara; Ansari, Junaid; Senchenkova, Elena Y. et al.
In: Dalton Transactions, Vol. 48, No. 44, 28.11.2019, p. 16764-16775.

Research output: Contribution to Journal/MagazineJournal articlepeer-review

Harvard

Boltersdorf, T, Ansari, J, Senchenkova, EY, Jiang, L, White, AJP, Coogan, M, Gavins, FNE & Long, NJ 2019, 'Development, characterisation and in vitro evaluation of lanthanide-based FPR2/ALX-targeted imaging probes', Dalton Transactions, vol. 48, no. 44, pp. 16764-16775. https://doi.org/10.1039/c9dt03520f

APA

Boltersdorf, T., Ansari, J., Senchenkova, E. Y., Jiang, L., White, A. J. P., Coogan, M., Gavins, F. N. E., & Long, N. J. (2019). Development, characterisation and in vitro evaluation of lanthanide-based FPR2/ALX-targeted imaging probes. Dalton Transactions, 48(44), 16764-16775. https://doi.org/10.1039/c9dt03520f

Vancouver

Boltersdorf T, Ansari J, Senchenkova EY, Jiang L, White AJP, Coogan M et al. Development, characterisation and in vitro evaluation of lanthanide-based FPR2/ALX-targeted imaging probes. Dalton Transactions. 2019 Nov 28;48(44):16764-16775. Epub 2019 Oct 25. doi: 10.1039/c9dt03520f

Author

Boltersdorf, Tamara ; Ansari, Junaid ; Senchenkova, Elena Y. et al. / Development, characterisation and in vitro evaluation of lanthanide-based FPR2/ALX-targeted imaging probes. In: Dalton Transactions. 2019 ; Vol. 48, No. 44. pp. 16764-16775.

Bibtex

@article{708ff0c2f1234aaf81bddd74d2550d28,
title = "Development, characterisation and in vitro evaluation of lanthanide-based FPR2/ALX-targeted imaging probes",
abstract = "We report the design, preparation and characterisation of three small-molecule, Formyl Peptide Receptor (FPR)-targeted lanthanide complexes (Tb·14, Eu·14 and Gd·14). Long-lived, metal-based emission was observed from the terbium complex (τH2O = 1.9 ms), whereas only negligible lanthanide signals were detected in the europium analogue. Ligand-centred emission was investigated using Gd·14 at room temperature and 77 K, leading to the postulation that metal emission may be sensitised via a ligand-based charge transfer state of the targeting Quin C1 unit. Comparatively high longitudinal relaxivity values (r1) for octadentate metal complexes of Gd·14 were determined (6.9 mM−1 s−1 at 400 MHz and 294 K), which could be a result of a relative increase in twisted square antiprism (TSAP) isomer prevalence compared to typical DOTA constructs (as evidenced by NMR spectroscopy). In vitro validation of concentration responses of Tb·14via three key neutrophil functional assays demonstrated that the inflammatory responses of neutrophils (i.e. chemotaxis, transmigration and granular release) remained unchanged in the presence of specific concentrations of the compound. Using a time-resolved microscopy set-up we were able to observe binding of the Tb·14 probe to stimulated human neutrophils around the cell periphery, while in the same experiment with un-activated neutrophils, no metal-based signals were detected. Our results demonstrate the utility of Tb·14 for time-resolved microscopy with lifetimes several orders of magnitude longer than autofluorescent signals and a preferential uptake in stimulated neutrophils.",
author = "Tamara Boltersdorf and Junaid Ansari and Senchenkova, {Elena Y.} and Lijun Jiang and White, {Andrew J. P.} and Michael Coogan and Gavins, {Felicity N. E.} and Long, {Nicholas J.}",
note = "{\textcopyright} Royal Society of Chemistry 2020",
year = "2019",
month = nov,
day = "28",
doi = "10.1039/c9dt03520f",
language = "English",
volume = "48",
pages = "16764--16775",
journal = "Dalton Transactions",
issn = "1477-9226",
publisher = "Royal Society of Chemistry",
number = "44",

}

RIS

TY - JOUR

T1 - Development, characterisation and in vitro evaluation of lanthanide-based FPR2/ALX-targeted imaging probes

AU - Boltersdorf, Tamara

AU - Ansari, Junaid

AU - Senchenkova, Elena Y.

AU - Jiang, Lijun

AU - White, Andrew J. P.

AU - Coogan, Michael

AU - Gavins, Felicity N. E.

AU - Long, Nicholas J.

N1 - © Royal Society of Chemistry 2020

PY - 2019/11/28

Y1 - 2019/11/28

N2 - We report the design, preparation and characterisation of three small-molecule, Formyl Peptide Receptor (FPR)-targeted lanthanide complexes (Tb·14, Eu·14 and Gd·14). Long-lived, metal-based emission was observed from the terbium complex (τH2O = 1.9 ms), whereas only negligible lanthanide signals were detected in the europium analogue. Ligand-centred emission was investigated using Gd·14 at room temperature and 77 K, leading to the postulation that metal emission may be sensitised via a ligand-based charge transfer state of the targeting Quin C1 unit. Comparatively high longitudinal relaxivity values (r1) for octadentate metal complexes of Gd·14 were determined (6.9 mM−1 s−1 at 400 MHz and 294 K), which could be a result of a relative increase in twisted square antiprism (TSAP) isomer prevalence compared to typical DOTA constructs (as evidenced by NMR spectroscopy). In vitro validation of concentration responses of Tb·14via three key neutrophil functional assays demonstrated that the inflammatory responses of neutrophils (i.e. chemotaxis, transmigration and granular release) remained unchanged in the presence of specific concentrations of the compound. Using a time-resolved microscopy set-up we were able to observe binding of the Tb·14 probe to stimulated human neutrophils around the cell periphery, while in the same experiment with un-activated neutrophils, no metal-based signals were detected. Our results demonstrate the utility of Tb·14 for time-resolved microscopy with lifetimes several orders of magnitude longer than autofluorescent signals and a preferential uptake in stimulated neutrophils.

AB - We report the design, preparation and characterisation of three small-molecule, Formyl Peptide Receptor (FPR)-targeted lanthanide complexes (Tb·14, Eu·14 and Gd·14). Long-lived, metal-based emission was observed from the terbium complex (τH2O = 1.9 ms), whereas only negligible lanthanide signals were detected in the europium analogue. Ligand-centred emission was investigated using Gd·14 at room temperature and 77 K, leading to the postulation that metal emission may be sensitised via a ligand-based charge transfer state of the targeting Quin C1 unit. Comparatively high longitudinal relaxivity values (r1) for octadentate metal complexes of Gd·14 were determined (6.9 mM−1 s−1 at 400 MHz and 294 K), which could be a result of a relative increase in twisted square antiprism (TSAP) isomer prevalence compared to typical DOTA constructs (as evidenced by NMR spectroscopy). In vitro validation of concentration responses of Tb·14via three key neutrophil functional assays demonstrated that the inflammatory responses of neutrophils (i.e. chemotaxis, transmigration and granular release) remained unchanged in the presence of specific concentrations of the compound. Using a time-resolved microscopy set-up we were able to observe binding of the Tb·14 probe to stimulated human neutrophils around the cell periphery, while in the same experiment with un-activated neutrophils, no metal-based signals were detected. Our results demonstrate the utility of Tb·14 for time-resolved microscopy with lifetimes several orders of magnitude longer than autofluorescent signals and a preferential uptake in stimulated neutrophils.

U2 - 10.1039/c9dt03520f

DO - 10.1039/c9dt03520f

M3 - Journal article

VL - 48

SP - 16764

EP - 16775

JO - Dalton Transactions

JF - Dalton Transactions

SN - 1477-9226

IS - 44

ER -