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  • 101.
    ter Veen, Rik
    et al.
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Surface Biotechnology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Physical and Analytical Chemistry.
    Fromell, Karin
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Surface Biotechnology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Physical and Analytical Chemistry.
    Caldwell, Karin
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Surface Biotechnology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Physical and Analytical Chemistry.
    Shifts in polystyrene particle surface charge upon adsorption of the Pluronic F108 surfactant2005In: Journal of Colloid and Interface Science, Vol. 288, no 1, p. 124-128Article in journal (Refereed)
    Abstract [en]

    Electrical field-flow fractionation (ElFFF) and sedimentation field-flow fractionation (SdFFF) were used in combination to study the adsorption of the triblock polymeric surfactant, Pluronic F108 [(EO)129-(PO)56-(EO)129] to 200 nm polystyrene (PS) latex spheres. The SdFFF technique allowed an accurate determination of the mass of surfactant adsorbed on each particle from a solution of given concentration. To complement this isotherm study, we show that ElFFF can be used to measure fractional coverages of the formed electrically neutral surfactant layers on the charged PS particles. Through a combination of the two techniques it is possible to gain information about the structure of the adsorbate layer. Thus, when Pluronic F108 is taken up by the PS surface from solutions of low concentration, all three blocks appear to adhere to the surface as long as there is free space available. As the solution concentration increases and the fractional coverage reaches approximately 20%, the surface turns crowded enough to let the strongly adsorbing PPO blocks competitively displace the weakly adherent PEO blocks, which gradually rise to extend into the aqueous phase until the surface is fully saturated.

  • 102. Valle-Delgado, J. J.
    et al.
    Molina-Bolivar, J. A.
    Galisteo-Gonzalez, F.
    Galvez-Ruiz, M. J.
    Feiler, A.
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Surface Biotechnology. Department of Physical and Analytical Chemistry, Surface Biotechnology.
    Rutland, M. W.
    Interaction Forces between BSA Layers Adsorbed on Silica Surfaces Measured with an Atomic Force Microscope2004In: J. Phys. Chem. B., Vol. 108, no 17, p. 5365-5371Article in journal (Refereed)
    Abstract [en]

    The interaction forces between bovine serum albumin (BSA) layers adsorbed on silica surfaces have been measured using an atomic force microscope (AFM) in conjunction with the colloid probe technique. Measurements of force-distance curves were made at different pH values and electrolyte concentrations (NaCl and CaCl2). The interaction at long range is dominated by electrical double-layer forces, while at short surface separations an additional repulsion due to the compression of the adsorbed protein layers appears. However, prior to this steric interaction, when the pH is above the isoelectric point of the protein and at high salt concentration, a non-DLVO repulsive interaction is observed. This behavior is explained if the presence of hydration forces in the system is assumed. Theoretical predictions including a hydration term in the DLVO theory fit the experimental results satisfactorily. The results presented in this article provide a direct confirmation that the AFM colloid probe technique can provide a useful way of directly quantifying the interaction of biological macromolecules.

  • 103. Valle-Delgado, J. J.
    et al.
    Molina-Bolivar, J. A.
    Galisteo-Gonzalez, F.
    Galvez-Ruiz, M. J.
    Feiler, Adam
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Surface Biotechnology. Department of Physical and Analytical Chemistry, Surface Biotechnology.
    Rutland, M. W.
    Existence of Hydration Forces in the Interaction between Apoferritin Molecules Adsorbed on Silica Surfaces2005In: Langmuir, Vol. 21, no 21, p. 9544-9554Article in journal (Refereed)
    Abstract [en]

    The atomic force microscope, together with the colloid probe technique, has become a very useful instrument to measure interaction forces between two surfaces. Its potential has been exploited in this work to study the interaction between protein (apoferritin) layers adsorbed on silica surfaces and to analyze the effect of the medium conditions (pH, salt concentration, salt type) on such interactions. It has been observed that the interaction at low salt concentrations is dominated by electrical double layer (at large distances) and steric forces (at short distances), the latter being due to compression of the protein layers. The DLVO theory fits these experimental data quite well. However, a non-DLVO repulsive interaction, prior to contact of the protein layers, is observed at high salt concentration above the isoelectric point of the protein. This behavior could be explained if the presence of hydration forces in the system is assumed. The inclusion of a hydration term in the DLVO theory (extended DLVO theory) gives rise to a better agreement between the theoretical fits and the experimental results. These results seem to suggest that the hydration forces play a very important role in the stability of the proteins in the physiological media.

  • 104. Valle-Delgado, J. J.
    et al.
    Molina-Bolívar, J. A.
    Galisteo-González, F.
    Gálvez-Ruiz, M. J.
    Feiler, A.
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Surface Biotechnology. Department of Physical and Analytical Chemistry, Surface Biotechnology.
    Rutland, M. W.
    Measurement of interactions between protein layers adsorbed on silica by atomic force microscopy2004In: J. Phys.: Condens. Matter, Vol. 16, no 26, p. 2383-2392Article in journal (Refereed)
    Abstract [en]

    The present work, using an atomic force microscope and the colloid probe technique, investigates the interaction forces between bovine serum albumin (BSA) layers and between apoferritin layers adsorbed on silica surfaces. The measurements have been carried out in an aqueous medium at different pH values and NaCl concentrations. Similar behaviours have been found with both proteins. Electrostatic and steric forces dominate the interactions between the protein layers at low NaCl concentrations. However, a very strange behaviour is found as a function of pH at high NaCl concentrations. The results obtained under these conditions could be explained if the presence of hydration forces in these systems is assumed.

  • 105. Valle-Delgado, J. J.
    et al.
    Molina-Bolívar, J. A.
    Galisteo-González, F.
    Gálvez-Ruiz, M. J.
    Feiler, Adam
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Surface Biotechnology. Department of Physical and Analytical Chemistry, Surface Biotechnology.
    Rutland, M. W.
    Hydration forces between silica surfaces: Experimental data and predictions from different theories2005In: The Journal of Chemical Physics, Vol. 123, p. 034708-Article in journal (Refereed)
    Abstract [en]

    Silica is a very interesting system that has been thoroughly studied in the last decades. One of the most outstanding characteristics of silica suspensions is their stability in solutions at high salt concentrations. In addition to that, measurements of direct-interaction forces between silica surfaces, obtained by different authors by means of surface force apparatus or atomic force microscope (AFM), reveal the existence of a strong repulsive interaction at short distances (below 2 nm) that decays exponentially. These results cannot be explained in terms of the classical Derjaguin, Landau, Verwey, and Overbeek (DLVO) theory, which only considers two types of forces: the electrical double-layer repulsion and the London–van der Waals attraction. Although there is a controversy about the origin of the short-range repulsive force, the existence of a structured layer of water molecules at the silica surface is the most accepted explanation for it. The overlap of structured water layers of different surfaces leads to repulsive forces, which are known as hydration forces. This assumption is based on the very hydrophilic nature of silica. Different theories have been developed in order to reproduce the exponentially decaying behavior (as a function of the separation distance) of the hydration forces. Different mechanisms for the formation of the structured water layer around the silica surfaces are considered by each theory. By the aid of an AFM and the colloid probe technique, the interaction forces between silica surfaces have been measured directly at different pH values and salt concentrations. The results confirm the presence of the short-range repulsion at any experimental condition (even at high salt concentration). A comparison between the experimental data and theoretical fits obtained from different theories has been performed in order to elucidate the nature of this non-DLVO repulsive force.

  • 106. Valle-Delgado, Juan José
    et al.
    Molina-Bolívar, José Antonio
    Galisteo-González, Francisco
    Gálvez-Ruiz, María José
    Feiler, Adam
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Surface Biotechnology. Department of Physical and Analytical Chemistry, Surface Biotechnology.
    Rutland, Mark
    Interactions between bovine serum albumin layers adsorbed on different substrates measured with an atomic force microscope2004In: Phys. Chem. Chem. Phys., Vol. 6, no 7, p. 1482-1486Article in journal (Refereed)
    Abstract [en]

    By the aid of an atomic force microscope (AFM) and the colloid probe technique, the interaction forces between bovine serum albumin (BSA) layers adsorbed on different substrates (silica and polystyrene) have been measured directly as a function of pH and salt concentration. Electrostatic and steric forces dominate the interactions at low salt concentrations. At high salt concentrations, when electrostatic interactions are screened, a very strange behaviour is found as a function of pH. The behaviour around the i.e.p. of the protein is also very striking: the interaction is attractive at low salt concentration, but it is repulsive at high salt concentration. These results could be explained if the presence of hydration forces is assumed. Theoretical predictions including a hydration term in the DLVO theory fit the experimental results satisfactorily.

  • 107.
    Veen, R
    et al.
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Surface Biotechnology. Technology, Department of Engineering Sciences, Electronics. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Physical and Analytical Chemistry.
    Jönsson, Mats
    Department of Materials Science. Technology, Department of Engineering Sciences, Electronics. Fasta tillståndets elektronik.
    Gantelius, J
    Lindberg, Ulf
    Department of Materials Science. Technology, Department of Engineering Sciences, Electronics. Fasta tillståndets elektronik.
    Caldwell, Karin
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Surface Biotechnology. Technology, Department of Engineering Sciences, Electronics. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Physical and Analytical Chemistry.
    Development of a micronized Electrical Field-Flow Fractionation instrument with an improved electrode system2003In: The 225th ACS National Meeting, Elopto 2003, March 24-27, New Orleans, USA, 2003Conference paper (Refereed)
  • 108. Walpole, Andrew R.
    et al.
    Briggs, E. P.
    Karlsson, Marjam
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Surface Biotechnology.
    Pålsgård, Eva
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Surface Biotechnology.
    Wilshaw, P. R.
    Nano-porous Alumina Coatings for Improved Bone Implant Interfaces2003In: Materialwissenschaft und Werkstofftechnik, ISSN 0933-5137, E-ISSN 1521-4052, Vol. 34, no 12, p. 1064-1068Article in journal (Refereed)
    Abstract [en]

    A new method is proposed for coating implants that produces a metal implant covered in a layer of nano-porous alumina ceramic. These layers are produced by first depositing a layer of aluminium on the implant surface and then anodising it in phosphoric acid to produce the nano-porous structure. This process results in the conversion of the aluminium to alumina containing 6-8wt% phosphate ions. The surface alumina layer is bonded to the substrate via an interfacial layer of fully dense anodised titanium oxide. Mechanical measurements have shown that the shear and tensile strength of this coating are in excess of 20MPa and 10MPa, respectively.

    The biological performance of nano-porous alumina material has been assessed and shown to be highly favourable, supporting normal osteoblastic activity and maintaining the osteoblastic phenotype. The filling of the nano-porous coating with bioactive material to achieve enhanced biological performance has been investigated using colloidal silica as an analogue for a Bioglass sol. The coating has been loaded with silica by dipping in colloidal silica with a pH of 5.6. Pore filling equivalent to 1.3 wt% SiO2 in the coating as a whole has been achieved in this way.

  • 109.
    Xu, Bingze
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Surface Biotechnology.
    Endoglucanase and Mannanase from Blue Mussel, Mytilus edulis: Purification, Characterization, Gene and Three Dimensional Structure2002Doctoral thesis, comprehensive summary (Other academic)
    Abstract [en]

    Two polysaccharide-degrading enzymes (endo-1,4-D-glucanase and β-mannanase) from blue mussel, Mytilus edulis, have been purified to homogeneity using a combination of several chromatographic steps. Each enzyme has been characterized with regard to its molecular weight, isoelectric point, pH and temperature stability, pH and temperature optimum and substrate specificity. The amino acid sequence of the endoglucanase has been determined at the protein level. The two enzymes are true blue mussel proteins as confirmed at the DNA level. The nucleotide sequences of synthesized cDNA from digestive gland and of genomic DNA from gill tissue were compared. Both genes contain introns, a property typical of eucaryotic organisms. Amino acid sequence based classification has revealed that the endoglucanase belongs to the glycoside hydrolase family 45, subfamily 2 while β-mannanase is a member of family 5.

    Both enzymes form insoluble inclusion bodies when expressed in Escherichia coli. Refolding attempts were unsuccessful. However, the β-mannanase was successfully expressed in the methylotropic yeast Pichia pastoris with an expression level above 100 mg/l in shaking culture. Crystals of the endoglucanase were made from the native protein and a dataset was collected to 1.85 Å resolution using an in-house rotating anode x-ray source. Crystals were also produced using recombinant β-mannanase and a dataset was collected to 1.4 Å resolution at the ESRF synchrotron beamline ID14-EH1. The three dimensional structure of the endoglucanase was solved by X-ray crystallography.

  • 110. Xu, J.
    et al.
    Sandström, C.
    Janson, Jan-Christer
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Surface Biotechnology.
    Tan, T.
    Chromatographic retention of epigallocatechin gallate on oligo-beta-cycloclextrin coupled sepharose media investigated using NMR2006In: Chromatographia, ISSN 0009-5893, E-ISSN 1612-1112, Vol. 64, no 1-2, p. 7-11Article in journal (Refereed)
    Abstract [en]

    The retention of epigallocatechin gallate (EGCG) on oligo-β-cyclodextrin (oligo-β-CD) bonded agarose chromatographic media was investigated. NMR spectroscopy in solution showed that the EGCG immerses into the β-CD cavity. The association constant calculated by NMR titration was used to estimate a retention factor which accurately reflected chromatographic behaviour. This correlation suggests that oligo-β-CD forms inclusion complexes with EGCG via the same mechanism as monomeric β-CD.

  • 111. Xu, Jun
    et al.
    Zhang, Guifeng
    Tan, Tianwei
    Janson, Jan-Christer
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Surface Biotechnology. Department of Physical and Analytical Chemistry, Surface Biotechnology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Physical and Analytical Chemistry.
    One-step purification of epigallocatechin gallate from crude green tea extracts by isocratic hydrogen bond adsorption chromatography on β-cyclodextrin substituted agarose gel media2005In: Journal of Chromatography B, Vol. 824, no 1-2, p. 323-326Article in journal (Refereed)
    Abstract [en]

    An oligomerized β-cyclodextrin ligand coupled to brominated allyl-group substituted Sepharose HP has been used for the one-step purification of polyphenolic epigallocatechin gallate (EGCG), an important antioxidant, by isocratic hydrogen bond adsorption chromatography. With a sample load of 1.33 mg crude green tea polyphenolic extract per ml column packing and with water/ethanol/acetonitrile (57/30/13, v/v) as the optimum mobile phase, an EGCG purity of about 98% with a recovery of approximate 73% could be achieved by proper peak cutting. After about 10 sample applications, the column performance started to deteriorate but could be regenerated to its original function by cleaning with 0.35 M NaOH.

  • 112. Xue, Bo
    et al.
    Ersson, Bo
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Surface Biotechnology. Department of Physical and Analytical Chemistry, Surface Biotechnology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Physical and Analytical Chemistry.
    Porath, Jerker
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Surface Biotechnology. Department of Physical and Analytical Chemistry, Surface Biotechnology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Physical and Analytical Chemistry.
    Caldwell, Karin
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Surface Biotechnology. Department of Physical and Analytical Chemistry, Surface Biotechnology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Physical and Analytical Chemistry.
    Chromatographic and fluorometric study of interactions between thiophilic and hydrophobic ligands and tryptophan peptide homologues2006In: Journal of Chromatography A, Vol. 1107, no 1-2, p. 46-51Article in journal (Refereed)
    Abstract [en]

    The interactions of tryptophan and its peptide homologues with thiophilic ligands were studied in terms of their chromatographic retention and steady-state fluorescence under various conditions, and compared with non-polar structures typically regarded as pure hydrophobic ligands. The experimental results show that both non-polar and polar interactions are involved in what has been termed “thiophilic adsorption chromatography”.

  • 113. Zhou, Weibin
    et al.
    Bi, Jingxiu
    Janson, Jan-Christer
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Surface Biotechnology. Department of Physical and Analytical Chemistry, Surface Biotechnology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Physical and Analytical Chemistry.
    Dong, Aihua
    Li, Yan
    Zhang, Yan
    Huang, Yongdong
    Su, Zhiguo
    Ion-exchange chromatography of hepatitis B virus surface antigen from a recombinant Chinese hamster ovary cell line2005In: Journal of Chromatography A, Vol. 1095, no 1-2, p. 119-125Article in journal (Refereed)
    Abstract [en]

    About 10% of the Chinese population are chronic carriers of hepatitis B virus (HBV). Thus, the development of a highly efficient process for the preparation of a vaccine based on a recombinant hepatitis B surface antigen (HBsAg) is very important to the Chinese national immunization program. To this end, the ion exchange chromatography recovery of CHO-HBsAg from a recombinant Chinese hamster ovary cell line was shown to increase from about 55 to 80% by the addition of 1% poly(ethylene glycol) (PEG 10,000) to the mobile phase. Furthermore, based on analysis by sodium dodecyl sulphate–polyacrylamide gel electrophoresis (SDS-PAGE), the intact glycoprotein form of CHO-HBsAg was completely preserved by the addition of PEG. In the absence of PEG the glycoprotein form of CHO-HBsAg was also spread out into the high salt elution fraction. High-performance size-exclusion chromatography with on-line multiangle-laser-light scattering (HPSEC-MALLS) analysis was performed to monitor the status of the CHO-HBsAg aggregate structure assembly, particle size and molecular weight distribution after each purification step, and the results showed further that the presence of PEG facilitated the separation and recovery of intact glycoprotein form of CHO-HBsAg and promoted their assembly to proper virus-like particles, which are both important features and prerequisites of their immunogenicity.

  • 114.
    Åhlund, John
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Physics, Department of Physics, Physics V.
    Nilson, Katharina
    Uppsala University, Disciplinary Domain of Science and Technology, Physics, Department of Physics, Physics V.
    Schiessling, Joachim
    Uppsala University, Disciplinary Domain of Science and Technology, Physics, Department of Physics, Physics V.
    Kjeldgaard, Lisbeth
    Berner, Simon
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Surface Biotechnology. Uppsala University, Disciplinary Domain of Science and Technology, Physics, Department of Physics, Physics V.
    Mårtensson, Nils
    Uppsala University, Disciplinary Domain of Science and Technology, Physics, Department of Physics, Physics V.
    Puglia, Carla
    Uppsala University, Disciplinary Domain of Science and Technology, Physics, Department of Physics, Physics V.
    Brena, Barbara
    Nyberg, Mats
    Luo, Yi
    The electronic structure of iron phthalocyanine probed by photoelectron and x-ray absorption spectroscopies and density functional theory calculations2006In: Journal of Chemical Physics, ISSN 0021-9606, E-ISSN 1089-7690, ISSN 0021-9606, Vol. 125, no 3, p. 34709-Article in journal (Refereed)
    Abstract [en]

    A joint experimental and theoretical work to explain the electronic and geometrical structure of anin situ prepared film of iron phthalocyanine FePc on silicon 100 is presented. FePc molecularfilms have been characterized by core and valence photoemission spectroscopy PES and x-rayabsorption spectroscopy XAS, and the results have been interpreted and simulated by densityfunctional theory DFT calculations. C1s and N1s PE spectra have been analyzed by taking intoaccount all chemically nonequivalent C and N atoms in the molecule. In the Fe2p3/2 spectra it hasbeen possible to resolve two components that can be related to the open shell structure of themolecule. By valence PES and N1s XAS data, the geometrical orientation of the FePc molecules inthe film could be determined. Our results indicate that for the FePc on Si100, the molecules withinthe film are mainly standing on the surface. The experimental N1s XAS spectra are very wellreproduced by the theoretical calculations, which are both angle and atomic resolved, giving adetailed description of the electronic and geometric structure of the FePc film. Furthermore, theasymmetry and the intensity angle variation of the first N1s XAS threshold feature could beexplained by the presented DFT calculations as due to the chemical nonequivalence of the N atomsand the symmetry character of the lowest unoccupied molecular orbital. © 2006 American Instituteof Physics.

  • 115.
    Örnskov, Eivor
    et al.
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Chemistry.
    Ullsten, Sara
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Chemistry.
    Söderberg, Lennart
    Surface Biotechnology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Physical and Analytical Chemistry.
    Markides, Karin
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Chemistry.
    Folestad, Staffan
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Chemistry.
    Method for immobilization of liposomes in capillary electrophoresis by electrostatic interaction with derivatized agarose2002In: Electrophoresis, ISSN 3381-3384, Vol. 23, p. 3381-3384Article in journal (Refereed)
    Abstract [en]

    A novel procedure for immobilization of liposomes inside fused-silica capillaries is

    demonstrated. First, the inner wall of the capillaries was coated with a positively

    charged polymer, composed of derivatized agarose. Subsequently, negatively charged

    liposomes were immobilized by electrostatic interaction on the polymer coating. The

    developed liposome coated capillaries were used as a nanoseparation tool for studying

    interactions between small drug compounds and liposomes. Part of this work was

    presented at the 15th International Symposium on Microscale Separations and Analysis,

    HPCE 2002, Stockholm, Sweden, April 2002.

123 101 - 115 of 115
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