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Influence of Glycosylation on Interfacial Properties of Recombinant Mucins: Adsorption, Surface Forces, and Friction
KTH Royal Institute of Technology, Sweden.
Sahlgrenska Academy, Sweden; University of Gothenburg, Sweden.
RISE - Research Institutes of Sweden, Biovetenskap och material, Kemi och material. KTH Royal Institute of Technology, Sweden.
Sahlgrenska Academy, Sweden; University of Gothenburg, Sweden.
Vise andre og tillknytning
2017 (engelsk)Inngår i: Langmuir, ISSN 0743-7463, E-ISSN 1520-5827, Vol. 33, nr 18, s. 4386-4395Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

Interfacial properties of two brush-with-anchor mucins, C-P55 and C-PSLex, have been investigated at the aqueous solution/poly(methyl methacrylate) (PMMA) interface. Both are recombinant mucin-type fusion proteins, produced by fusing the glycosylated mucin part of P-selectin glycoprotein ligand-1 (PSLG-1) to the Fc part of a mouse immunoglobulin in two different cells. They are mainly expressed as dimers upon production. Analysis of the O-glycans shows that the C-PSLex mucin has the longer and more branched side chains, but C-P55 has slightly higher sialic acid content. The adsorption of the mucins to PMMA surfaces was studied by quartz crystal microbalance with dissipation. The sensed mass, including the adsorbed mucin and water trapped in the layer, was found to be similar for these two mucin layers. Atomic force microscopy with colloidal probe was employed to study surface and friction forces between mucin-coated PMMA surfaces. Purely repulsive forces of steric origin were observed between mucin layers on compression, whereas a small adhesion was detected between both mucin layers on decompression. This was attributed to chain entanglement. The friction force between C-PSLex-coated PMMA is lower than that between C-P55-coated PMMA at low loads, but vice versa at high loads. We discuss our results in terms of the differences in the glycosylation composition of these two mucins.

sted, utgiver, år, opplag, sider
American Chemical Society , 2017. Vol. 33, nr 18, s. 4386-4395
Emneord [en]
Atomic force microscopy, Chains, Esters, Glycosylation, Proteins, Recombinant proteins, Solutions, Tribology, Branched side chains, Chain entanglements, Colloidal probes, Interfacial property, Methyl methacrylates, P-selectin glycoprotein ligand-1, Quartz crystal microbalance with dissipation, Repulsive forces, Friction
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Identifikatorer
URN: urn:nbn:se:ri:diva-29773DOI: 10.1021/acs.langmuir.7b00030Scopus ID: 2-s2.0-85019122835OAI: oai:DiVA.org:ri-29773DiVA, id: diva2:1108414
Forskningsfinansiär
Knut and Alice Wallenberg FoundationSwedish Research Council
Merknad

Funding details: Australian Liver Foundation; Funding details: Swedish Foundation for International Cooperation in Research and Higher Education;

Tilgjengelig fra: 2017-06-12 Laget: 2017-06-12 Sist oppdatert: 2019-01-03bibliografisk kontrollert

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