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Change of Colloidal...
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Hedlund, Julia,1975Gothenburg University,Göteborgs universitet,Institutionen för cell- och molekylärbiologi,Department of Cell and Molecular Biology
(author)
Change of Colloidal and Surface Properties of Mytilus edulis Foot Protein 1 in the Presence of an Oxidation (NaIO4) or a Complex-Binding (Cu2+) Agent
- Article/chapterEnglish2009
Publisher, publication year, extent ...
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2009-02-11
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American Chemical Society (ACS),2009
Numbers
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LIBRIS-ID:oai:gup.ub.gu.se/104950
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https://gup.ub.gu.se/publication/104950URI
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https://doi.org/10.1021/bm801325jDOI
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Subject category:ref swepub-contenttype
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Subject category:art swepub-publicationtype
Notes
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Quartz crystal microbalance with dissipation monitoring (QCM-D) was used to study the viscoelastic properties of the blue mussel, Mytilus edulis, foot protein 1 (Mefp-1) adsorbed on modified hydrophobic gold surfaces. The change in viscoelasticity was studied after addition of Cu2+ and Mn2+, which theoretically could induce metal complex formation with 3,4-dihydroxyphenylalanine (DOPA) moieties. We also used NaIO4, a nonmetal oxidative agent known to induce di-DOPA formation. Reduction in viscoelasticity of adsorbed Mefp-1 followed the order of NaIO4 > Cu2+ > buffer control > Mn2+. We also studied the formation of molecular aggregates of Mefp-1 in solution with the use of dynamic light scattering (DLS). We found that addition of Cu2+, but not Mn2+, induced the formation of larger DLS-detectable aggregates. Minor aggregate formation was found with NaIO4. With the analytical resolution of small angle X-ray scattering (SAXS), we could detect differences in the molecular structure between NaIO4- and Cu2+-treated Mefp-1 aggregates. We concluded from this study that Cu2+ could participate in intermolecular cross-linking of the Mefp-1 molecule via metal complex formation. Metal incorporation in the protein most likely increases the abrasion resistance of the Mefp-1 layer. NaIO4, on the other hand, resulted in mainly intramolecular formation of di-DOPA, but failed to induce larger intermolecular aggregation phenomena. The described methodological combination of surface sensitive methods, like QCM-D, and bulk sensitive methods, like DLS and SAXS, generates high resolution results and is an attractive platform to investigate intra- and intermolecular aspects of assembly and cross-linking of the Mefp proteins.
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Andersson, Marcus,1975Gothenburg University,Göteborgs universitet,Institutionen för cell- och molekylärbiologi,Department of Cell and Molecular Biology(Swepub:gu)xamarn
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Fant, C.
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Bitton, R.
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Bianco-Peled, H.
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Elwing, Hans-Björne,1946Gothenburg University,Göteborgs universitet,Institutionen för cell- och molekylärbiologi,Department of Cell and Molecular Biology(Swepub:gu)xelwha
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Berglin, Mattias,1970Gothenburg University,Göteborgs universitet,Institutionen för cell- och molekylärbiologi,Department of Cell and Molecular Biology(Swepub:gu)xbemat
(author)
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Göteborgs universitetInstitutionen för cell- och molekylärbiologi
(creator_code:org_t)
Related titles
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In:Biomacromolecules: American Chemical Society (ACS)10:4, s. 845-8491525-77971526-4602
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