Quantification of pharmaceutical peptides using selenium as an elemental detection label

Research output: Contribution to journalJournal articleResearchpeer-review

Standard

Quantification of pharmaceutical peptides using selenium as an elemental detection label. / Møller, Laura Hyrup; Gabel-Jensen, Charlotte; Franzyk, Henrik; Bahnsen, Jesper Søborg; Stürup, Stefan; Gammelgaard, Bente.

In: Metallomics : integrated biometal science, Vol. 6, 16.07.2014, p. 1639-1647.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Møller, LH, Gabel-Jensen, C, Franzyk, H, Bahnsen, JS, Stürup, S & Gammelgaard, B 2014, 'Quantification of pharmaceutical peptides using selenium as an elemental detection label', Metallomics : integrated biometal science, vol. 6, pp. 1639-1647. https://doi.org/10.1039/c4mt00085d

APA

Møller, L. H., Gabel-Jensen, C., Franzyk, H., Bahnsen, J. S., Stürup, S., & Gammelgaard, B. (2014). Quantification of pharmaceutical peptides using selenium as an elemental detection label. Metallomics : integrated biometal science, 6, 1639-1647. https://doi.org/10.1039/c4mt00085d

Vancouver

Møller LH, Gabel-Jensen C, Franzyk H, Bahnsen JS, Stürup S, Gammelgaard B. Quantification of pharmaceutical peptides using selenium as an elemental detection label. Metallomics : integrated biometal science. 2014 Jul 16;6:1639-1647. https://doi.org/10.1039/c4mt00085d

Author

Møller, Laura Hyrup ; Gabel-Jensen, Charlotte ; Franzyk, Henrik ; Bahnsen, Jesper Søborg ; Stürup, Stefan ; Gammelgaard, Bente. / Quantification of pharmaceutical peptides using selenium as an elemental detection label. In: Metallomics : integrated biometal science. 2014 ; Vol. 6. pp. 1639-1647.

Bibtex

@article{de96c161851e46acb57c91bbac9cbb3d,
title = "Quantification of pharmaceutical peptides using selenium as an elemental detection label",
abstract = "The aim of the present work was to demonstrate how selenium labelling of a synthetic cell-penetrating peptide may be employed in evaluation of stability and quantitative estimation of cellular uptake by inductively coupled plasma mass spectrometry (ICP-MS). Two analogues of the cell-penetrating peptide, penetratin, were synthesized, one with selenomethionine (SeMet) added at the N-terminal of the peptide (N-PenM(Se)) and the other with the internal methionine (Met) replaced with SeMet (i-PenM(Se)). The purity of the synthesized peptides was 92{\%} for N-PenM(Se) and 89{\%} for i-PenM(Se) as determined by liquid chromatography (LC)-ICP-MS. The selenium-labelled peptides were investigated by cell uptake studies in HeLa WT cells. The stability of the peptides was monitored in water, cell medium and during cell uptake studies. Total uptake of selenium was quantified by flow injection (FI)-ICP-MS. Speciation analysis of cell samples by LC-ICP-MS showed mainly uptake of the intact peptides, while the amount of intact peptides in cell lysates was semi-quantitatively determined. The selenium-containing penetratin analogues were to some extent degraded in pure cell medium, while an extensive degradation was observed during cell uptake studies. The major degradation products were determined by LC-electrospray ionization mass spectrometry (ESI-MS). The labelling method in combination with FI-ICP-MS, LC-ICP-MS and LC-ESI-MS techniques provided detailed information on the fate of penetratin in cellular uptake studies. Most pharmaceutical peptides, including penetratin, are synthetic analogues of endogenous peptides, and incorporation of selenium may improve the critical assessment of the native drug or drug delivery candidate early in the drug development process.",
author = "M{\o}ller, {Laura Hyrup} and Charlotte Gabel-Jensen and Henrik Franzyk and Bahnsen, {Jesper S{\o}borg} and Stefan St{\"u}rup and Bente Gammelgaard",
year = "2014",
month = "7",
day = "16",
doi = "10.1039/c4mt00085d",
language = "English",
volume = "6",
pages = "1639--1647",
journal = "Metallomics",
issn = "1756-5901",
publisher = "Royal Society of Chemistry",

}

RIS

TY - JOUR

T1 - Quantification of pharmaceutical peptides using selenium as an elemental detection label

AU - Møller, Laura Hyrup

AU - Gabel-Jensen, Charlotte

AU - Franzyk, Henrik

AU - Bahnsen, Jesper Søborg

AU - Stürup, Stefan

AU - Gammelgaard, Bente

PY - 2014/7/16

Y1 - 2014/7/16

N2 - The aim of the present work was to demonstrate how selenium labelling of a synthetic cell-penetrating peptide may be employed in evaluation of stability and quantitative estimation of cellular uptake by inductively coupled plasma mass spectrometry (ICP-MS). Two analogues of the cell-penetrating peptide, penetratin, were synthesized, one with selenomethionine (SeMet) added at the N-terminal of the peptide (N-PenM(Se)) and the other with the internal methionine (Met) replaced with SeMet (i-PenM(Se)). The purity of the synthesized peptides was 92% for N-PenM(Se) and 89% for i-PenM(Se) as determined by liquid chromatography (LC)-ICP-MS. The selenium-labelled peptides were investigated by cell uptake studies in HeLa WT cells. The stability of the peptides was monitored in water, cell medium and during cell uptake studies. Total uptake of selenium was quantified by flow injection (FI)-ICP-MS. Speciation analysis of cell samples by LC-ICP-MS showed mainly uptake of the intact peptides, while the amount of intact peptides in cell lysates was semi-quantitatively determined. The selenium-containing penetratin analogues were to some extent degraded in pure cell medium, while an extensive degradation was observed during cell uptake studies. The major degradation products were determined by LC-electrospray ionization mass spectrometry (ESI-MS). The labelling method in combination with FI-ICP-MS, LC-ICP-MS and LC-ESI-MS techniques provided detailed information on the fate of penetratin in cellular uptake studies. Most pharmaceutical peptides, including penetratin, are synthetic analogues of endogenous peptides, and incorporation of selenium may improve the critical assessment of the native drug or drug delivery candidate early in the drug development process.

AB - The aim of the present work was to demonstrate how selenium labelling of a synthetic cell-penetrating peptide may be employed in evaluation of stability and quantitative estimation of cellular uptake by inductively coupled plasma mass spectrometry (ICP-MS). Two analogues of the cell-penetrating peptide, penetratin, were synthesized, one with selenomethionine (SeMet) added at the N-terminal of the peptide (N-PenM(Se)) and the other with the internal methionine (Met) replaced with SeMet (i-PenM(Se)). The purity of the synthesized peptides was 92% for N-PenM(Se) and 89% for i-PenM(Se) as determined by liquid chromatography (LC)-ICP-MS. The selenium-labelled peptides were investigated by cell uptake studies in HeLa WT cells. The stability of the peptides was monitored in water, cell medium and during cell uptake studies. Total uptake of selenium was quantified by flow injection (FI)-ICP-MS. Speciation analysis of cell samples by LC-ICP-MS showed mainly uptake of the intact peptides, while the amount of intact peptides in cell lysates was semi-quantitatively determined. The selenium-containing penetratin analogues were to some extent degraded in pure cell medium, while an extensive degradation was observed during cell uptake studies. The major degradation products were determined by LC-electrospray ionization mass spectrometry (ESI-MS). The labelling method in combination with FI-ICP-MS, LC-ICP-MS and LC-ESI-MS techniques provided detailed information on the fate of penetratin in cellular uptake studies. Most pharmaceutical peptides, including penetratin, are synthetic analogues of endogenous peptides, and incorporation of selenium may improve the critical assessment of the native drug or drug delivery candidate early in the drug development process.

U2 - 10.1039/c4mt00085d

DO - 10.1039/c4mt00085d

M3 - Journal article

VL - 6

SP - 1639

EP - 1647

JO - Metallomics

T2 - Metallomics

JF - Metallomics

SN - 1756-5901

ER -

ID: 119249169