Publications by authors named "Camilla Fant"

The strategy of metal ion complexation is employed to design a delivery system for an antifouling agent (AFA) in marine paints. A poly(1-vinylimidazole-co-methyl methacrylate) copolymer (PVM), together with Cu2+ or Zn2+ formed a PVM-M2+ complex. The AFA, Medetomidine, was then coordinated into the complex.

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Five peptides: BPI(85-109); CAP18(106-137); endotoxin inhibitor (EI); GQ33 and GQ33C, derived from lipopolysaccharide (LPS)-binding molecules were investigated for LPS-binding ability with a view to a potential use in extracorporeal therapy. The surface plasmon resonance technique (SPR) was used to monitor the interaction between LPS in solution and the surface-immobilized peptides. The peptides were covalently bound to a model dextran surface via inherent amino groups or via terminally introduced cysteine residues.

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Hemoglobin (Hb) in single erythrocytes (red blood cells), adsorbed on polylysine-coated glass surfaces, was studied using resonance Raman spectroscopy and global Raman imaging. The erythrocytes were found to be sensitive to both surface adsorption and laser illumination. Substrate-dependent changes of the cell membrane shape were observed immediately after cell adsorption, while a photo-induced increase of fluorescence was observed for visible excitation (lambda=514.

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We have quantified surface associated coagulation of human blood plasma with a recently developed methodological system consisting of a Quartz Crystal Microbalance with Dissipation monitoring (QCM-D), a method that measures the weight of adsorbed molecules on surfaces as a function of frequency shifts of a quartz crystal. Further, it measures the damping energy (i.e.

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The interaction between two proteins, Mefp-1 and Mefp-2, from the byssal plaque of the blue mussel, Mytilus edulis, was investigated using a quartz crystal microbalance with dissipation monitoring (QCM-D) technique. The challenge in using a surface-sensitive technique to investigate the interaction between two strongly adhesive proteins was met by coupling a biotinylated version of one of the proteins (b-Mefp-1) to an inert two-dimensional arrangement of streptavidin (SA) formed on top of a biotin-doped supported phospholipid bilayer. The interaction between Mefp-1 and Mefp-2 was further investigated by addition of Mefp-2 to SA-coupled b-Mefp-1, where the latter was either in the native state or cross-linked using sodium periodate (NaIO(4)), Cu(2+), or mushroom tyrosinase.

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