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

Ashton, L., Pudney, P.D.A., Blanch, E.W. and Yakubov, G.E. (2013) Understanding glycoprotein behaviours using Raman and Raman optical activity spectroscopies: Characterising the entanglement induced conformational changes in oligosaccharide chains of mucin. Advances in Colloid and Interface Science, 199-200 66-77. doi:10.1016/j.cis.2013.06.005


Author Ashton, L.
Pudney, P.D.A.
Blanch, E.W.
Yakubov, G.E.
Title Understanding glycoprotein behaviours using Raman and Raman optical activity spectroscopies: Characterising the entanglement induced conformational changes in oligosaccharide chains of mucin
Journal name Advances in Colloid and Interface Science   Check publisher's open access policy
ISSN 0001-8686
1873-3727
Publication date 2013-11
Year available 2013
Sub-type Article (original research)
DOI 10.1016/j.cis.2013.06.005
Open Access Status
Volume 199-200
Start page 66
End page 77
Total pages 12
Place of publication Amsterdam, The Netherlands
Publisher Elsevier BV
Collection year 2014
Language eng
Subject 1505 Marketing
1606 Political Science
3110 Surfaces and Interfaces
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 ∼ 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 β-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.
Keyword 2D correlation analysis
Glycoprotein
Mucin
Polymer entanglement
Raman optical activity
Raman spectroscopy
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: School of Chemical Engineering Publications
Official 2014 Collection
 
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