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Understanding glycoprotein behaviours using Raman and Raman optical activity spectroscopies: characterising the entanglement induced conformational changes in oligosaccharide chains of mucin

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Understanding glycoprotein behaviours using Raman and Raman optical activity spectroscopies : characterising the entanglement induced conformational changes in oligosaccharide chains of mucin. / Ashton, Lorna; Pudney, P. D. A.; Blanch, E. W.; Yakubov, G. E.

In: Advances in Colloid and Interface Science, Vol. 199-200, 11.2013, p. 66-77.

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@article{4fe8a8021b214404bb39dda82249c5a2,
title = "Understanding glycoprotein behaviours using Raman and Raman optical activity spectroscopies: characterising the entanglement induced conformational changes in oligosaccharide chains of mucin",
abstract = "We illustrate the great potential of Raman and ROA spectroscopies for investigating the structure and organisation of glycoproteins and the complex matrices they can form. In combination these spectroscopic techniques are sensitive to changes in conformation revealing details of secondary and tertiary structures, probing hydrogen bonding interactions, as well as resolving side chain orientation and the absolute configuration of chiral substructures. To demonstrate this potential we have characterised the structural changes in a complex glycoprotein, mucin. Spectral changes were observed during the entanglement transition as the mucin concentration was increased. By applying two-dimensional correlation analysis (2DCos) to the ROA and Raman concentration-dependent spectral sets delicate transitions in mucin conformation could also be determined. From similar to 20-40 mg/ml conformational transitions assigned mainly to the sugar N-acetyl-D-galactosamine (GalNAc), which is the linking saccharide unit to the protein backbone, were monitored. Further changes in local oligosaccharide conformation above 40 mg/ml were also monitored, together with other structural transitions observed in the protein core, particularly beta-structure formation. Consequently, these spectral techniques were shown to monitor the formation of transient entanglements formed by brush-brush interactions between oligosaccharide combs of mucin molecules identifying changes in both carbohydrate and protein moieties. This work clearly shows how these methods can be used to elucidate fresh insights into the complex behaviour of these large complex molecules. (C) 2013 Elsevier B.V. All rights reserved.",
keywords = "Raman optical activity, Raman spectroscopy, Glycoprotein, Mucin, Polymer entanglement, 2D correlation analysis, 2-DIMENSIONAL CORRELATION SPECTROSCOPY, PORCINE STOMACH MUCIN, POLYPROLINE-II HELICES, UNFOLDED PROTEINS, RHEOLOGICAL PROPERTIES, SEQUENTIAL ORDER, ACTIVITY SPECTRA, NUCLEIC-ACIDS, GASTRIC MUCIN, D-GLUCOSE",
author = "Lorna Ashton and Pudney, {P. D. A.} and Blanch, {E. W.} and Yakubov, {G. E.}",
year = "2013",
month = nov,
doi = "10.1016/j.cis.2013.06.005",
language = "English",
volume = "199-200",
pages = "66--77",
journal = "Advances in Colloid and Interface Science",
issn = "0001-8686",
publisher = "Elsevier",

}

RIS

TY - JOUR

T1 - Understanding glycoprotein behaviours using Raman and Raman optical activity spectroscopies

T2 - characterising the entanglement induced conformational changes in oligosaccharide chains of mucin

AU - Ashton, Lorna

AU - Pudney, P. D. A.

AU - Blanch, E. W.

AU - Yakubov, G. E.

PY - 2013/11

Y1 - 2013/11

N2 - We illustrate the great potential of Raman and ROA spectroscopies for investigating the structure and organisation of glycoproteins and the complex matrices they can form. In combination these spectroscopic techniques are sensitive to changes in conformation revealing details of secondary and tertiary structures, probing hydrogen bonding interactions, as well as resolving side chain orientation and the absolute configuration of chiral substructures. To demonstrate this potential we have characterised the structural changes in a complex glycoprotein, mucin. Spectral changes were observed during the entanglement transition as the mucin concentration was increased. By applying two-dimensional correlation analysis (2DCos) to the ROA and Raman concentration-dependent spectral sets delicate transitions in mucin conformation could also be determined. From similar to 20-40 mg/ml conformational transitions assigned mainly to the sugar N-acetyl-D-galactosamine (GalNAc), which is the linking saccharide unit to the protein backbone, were monitored. Further changes in local oligosaccharide conformation above 40 mg/ml were also monitored, together with other structural transitions observed in the protein core, particularly beta-structure formation. Consequently, these spectral techniques were shown to monitor the formation of transient entanglements formed by brush-brush interactions between oligosaccharide combs of mucin molecules identifying changes in both carbohydrate and protein moieties. This work clearly shows how these methods can be used to elucidate fresh insights into the complex behaviour of these large complex molecules. (C) 2013 Elsevier B.V. All rights reserved.

AB - We illustrate the great potential of Raman and ROA spectroscopies for investigating the structure and organisation of glycoproteins and the complex matrices they can form. In combination these spectroscopic techniques are sensitive to changes in conformation revealing details of secondary and tertiary structures, probing hydrogen bonding interactions, as well as resolving side chain orientation and the absolute configuration of chiral substructures. To demonstrate this potential we have characterised the structural changes in a complex glycoprotein, mucin. Spectral changes were observed during the entanglement transition as the mucin concentration was increased. By applying two-dimensional correlation analysis (2DCos) to the ROA and Raman concentration-dependent spectral sets delicate transitions in mucin conformation could also be determined. From similar to 20-40 mg/ml conformational transitions assigned mainly to the sugar N-acetyl-D-galactosamine (GalNAc), which is the linking saccharide unit to the protein backbone, were monitored. Further changes in local oligosaccharide conformation above 40 mg/ml were also monitored, together with other structural transitions observed in the protein core, particularly beta-structure formation. Consequently, these spectral techniques were shown to monitor the formation of transient entanglements formed by brush-brush interactions between oligosaccharide combs of mucin molecules identifying changes in both carbohydrate and protein moieties. This work clearly shows how these methods can be used to elucidate fresh insights into the complex behaviour of these large complex molecules. (C) 2013 Elsevier B.V. All rights reserved.

KW - Raman optical activity

KW - Raman spectroscopy

KW - Glycoprotein

KW - Mucin

KW - Polymer entanglement

KW - 2D correlation analysis

KW - 2-DIMENSIONAL CORRELATION SPECTROSCOPY

KW - PORCINE STOMACH MUCIN

KW - POLYPROLINE-II HELICES

KW - UNFOLDED PROTEINS

KW - RHEOLOGICAL PROPERTIES

KW - SEQUENTIAL ORDER

KW - ACTIVITY SPECTRA

KW - NUCLEIC-ACIDS

KW - GASTRIC MUCIN

KW - D-GLUCOSE

U2 - 10.1016/j.cis.2013.06.005

DO - 10.1016/j.cis.2013.06.005

M3 - Journal article

VL - 199-200

SP - 66

EP - 77

JO - Advances in Colloid and Interface Science

JF - Advances in Colloid and Interface Science

SN - 0001-8686

ER -