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Detection of protein glycosylation using tip enhanced Raman scattering

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Detection of protein glycosylation using tip enhanced Raman scattering. / Cowcher, David; Deckert-Gaudig, Tanja ; Brewster, Victoria et al.

In: Analytical Chemistry, Vol. 88, No. 4, 16.02.2016, p. 2105-2112.

Research output: Contribution to Journal/MagazineJournal articlepeer-review

Harvard

Cowcher, D, Deckert-Gaudig, T, Brewster, V, Ashton, L, Deckert, V & Goodacre, R 2016, 'Detection of protein glycosylation using tip enhanced Raman scattering', Analytical Chemistry, vol. 88, no. 4, pp. 2105-2112. https://doi.org/10.1021/acs.analchem.5b03535

APA

Cowcher, D., Deckert-Gaudig, T., Brewster, V., Ashton, L., Deckert, V., & Goodacre, R. (2016). Detection of protein glycosylation using tip enhanced Raman scattering. Analytical Chemistry, 88(4), 2105-2112. https://doi.org/10.1021/acs.analchem.5b03535

Vancouver

Cowcher D, Deckert-Gaudig T, Brewster V, Ashton L, Deckert V, Goodacre R. Detection of protein glycosylation using tip enhanced Raman scattering. Analytical Chemistry. 2016 Feb 16;88(4):2105-2112. Epub 2016 Jan 25. doi: 10.1021/acs.analchem.5b03535

Author

Cowcher, David ; Deckert-Gaudig, Tanja ; Brewster, Victoria et al. / Detection of protein glycosylation using tip enhanced Raman scattering. In: Analytical Chemistry. 2016 ; Vol. 88, No. 4. pp. 2105-2112.

Bibtex

@article{a3f4e412226d47c2ab577ad4e06a9a0e,
title = "Detection of protein glycosylation using tip enhanced Raman scattering",
abstract = "The correct glycosylation of biopharmaceutical glycoproteins and their formulations is essential for them to have the desired therapeutic effect on the patient. It has recently been shown that Raman spectroscopy can be used to quantify the proportion of glycosylated protein from mixtures of native and glycosylated forms of bovine pancreatic ribonuclease (RNase). Here we show the first steps towards not only the detection of glycosylation status, but the characterisation of glycans themselves from just a few protein molecules at a time using tip-enhanced Raman scattering (TERS). Whilst this technique generates complex data that are very dependent on the protein orientation, with the careful development of combined data preprocessing, univariate and multivariate analysis techniques, we have shown that we can distinguish between the native and glycosylated forms of RNase. Many glycoproteins contain populations of subtly different glycoforms, therefore with stricter orientation control, we believe this has the potential to lead to further glycan characterisation using TERS, which would have use in biopharmaceutical synthesis and formulation research.",
author = "David Cowcher and Tanja Deckert-Gaudig and Victoria Brewster and Lorna Ashton and Volker Deckert and Royston Goodacre",
note = "ACS AuthorChoice - This is an open access article published under a Creative Commons Attribution (CC-BY) License, which permits unrestricted use, distribution and reproduction in any medium, provided the author and source are cited.",
year = "2016",
month = feb,
day = "16",
doi = "10.1021/acs.analchem.5b03535",
language = "English",
volume = "88",
pages = "2105--2112",
journal = "Analytical Chemistry",
issn = "0003-2700",
publisher = "American Chemical Society",
number = "4",

}

RIS

TY - JOUR

T1 - Detection of protein glycosylation using tip enhanced Raman scattering

AU - Cowcher, David

AU - Deckert-Gaudig, Tanja

AU - Brewster, Victoria

AU - Ashton, Lorna

AU - Deckert, Volker

AU - Goodacre, Royston

N1 - ACS AuthorChoice - This is an open access article published under a Creative Commons Attribution (CC-BY) License, which permits unrestricted use, distribution and reproduction in any medium, provided the author and source are cited.

PY - 2016/2/16

Y1 - 2016/2/16

N2 - The correct glycosylation of biopharmaceutical glycoproteins and their formulations is essential for them to have the desired therapeutic effect on the patient. It has recently been shown that Raman spectroscopy can be used to quantify the proportion of glycosylated protein from mixtures of native and glycosylated forms of bovine pancreatic ribonuclease (RNase). Here we show the first steps towards not only the detection of glycosylation status, but the characterisation of glycans themselves from just a few protein molecules at a time using tip-enhanced Raman scattering (TERS). Whilst this technique generates complex data that are very dependent on the protein orientation, with the careful development of combined data preprocessing, univariate and multivariate analysis techniques, we have shown that we can distinguish between the native and glycosylated forms of RNase. Many glycoproteins contain populations of subtly different glycoforms, therefore with stricter orientation control, we believe this has the potential to lead to further glycan characterisation using TERS, which would have use in biopharmaceutical synthesis and formulation research.

AB - The correct glycosylation of biopharmaceutical glycoproteins and their formulations is essential for them to have the desired therapeutic effect on the patient. It has recently been shown that Raman spectroscopy can be used to quantify the proportion of glycosylated protein from mixtures of native and glycosylated forms of bovine pancreatic ribonuclease (RNase). Here we show the first steps towards not only the detection of glycosylation status, but the characterisation of glycans themselves from just a few protein molecules at a time using tip-enhanced Raman scattering (TERS). Whilst this technique generates complex data that are very dependent on the protein orientation, with the careful development of combined data preprocessing, univariate and multivariate analysis techniques, we have shown that we can distinguish between the native and glycosylated forms of RNase. Many glycoproteins contain populations of subtly different glycoforms, therefore with stricter orientation control, we believe this has the potential to lead to further glycan characterisation using TERS, which would have use in biopharmaceutical synthesis and formulation research.

U2 - 10.1021/acs.analchem.5b03535

DO - 10.1021/acs.analchem.5b03535

M3 - Journal article

VL - 88

SP - 2105

EP - 2112

JO - Analytical Chemistry

JF - Analytical Chemistry

SN - 0003-2700

IS - 4

ER -