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  • 1.
    Grant, LM
    et al.
    YKI – Ytkemiska institutet.
    Tiberg, F
    YKI – Ytkemiska institutet.
    Normal and lateral forces between lipid covered solids in solution: Correlation with layer packing and structure2002In: Biophysical Journal, ISSN 0006-3495, E-ISSN 1542-0086, Vol. 82, p. 1373-1385Article in journal (Refereed)
    Abstract [en]

    We report on the normal and lateral forces between controlled-density mono- and bilayers of phospholipid co-adsorbed onto hydrophobic and hydrophilic solid supports, respectively. Interactions between 1,2-dioleoyl-sn-glycero-3-phosphocholine layers were measured using an atomic force microscope. Notable features of the normal force curves (barrier heights and widths) were found to correlate with the thickness and density of the supported lipid layers. The friction and normal force curves were also found interrelated. Thus, very low friction values were measured as long as the supported layer(s) resisted the normal pressure of the tip. However, as the applied load exceeded the critical value needed for puncturing the layers, the friction jumped to values close to those recorded between bare surfaces. The lipid layers were self-healing between measurements, but a significant hysteresis was observed in the force curves measured on approach and retraction, respectively. The study shows the potential of using atomic force microscopy for lipid layer characterization both with respect to structure and interactions. It further shows the strong lubricating effect of adsorbed lipid layers and how this varies with surface density of lipids. The findings may have important implications for the issue of joint lubrication.

  • 2. Liljeblad, Jonathan FD
    et al.
    Bulone, Vincent
    Tyrode, Eric
    Rutland, Mark W.
    RISE, SP – Sveriges Tekniska Forskningsinstitut, SP Sveriges tekniska forskningsinstitut, YKI – Ytkemiska institutet.
    Johnson, C Magnus
    Phospholipid monolayers probed by vibrational sum frequency spectroscopy: Instability of unsaturated phospholipids2010In: Biophysical Journal, ISSN 0006-3495, E-ISSN 1542-0086, Vol. 98, no 10, p. L50-Article in journal (Refereed)
    Abstract [en]

    The surface specific technique vibrational sum frequency spectroscopy has been applied to in situ studies of the degradation of Langmuir monolayers of 1, 2-diacyl-phosphocholines with various degrees of unsaturation in the aliphatic chains. To monitor the degradation of the phospholipids, the time-dependent change of the monolayer area at constant surface pressure and the sum frequency intensity of the vinyl CH stretch at the carbon-carbon double bonds were measured. The data show a rapid degradation of monolayers of phospholipids carrying unsaturated aliphatic chains compared to the stable lipids carrying fully saturated chains when exposed to the ambient laboratory air. In addition, the degradation of the phospholipids can be inhibited by purging the ambient air with nitrogen. This instability may be attributed to spontaneous degradation by oxidation mediated by various reactive species in the air. To further elucidate the process of lipid oxidation in biological membranes artificial Langmuir monolayers probed by a surface specific spectroscopic technique as in this study can serve as a model system for studying the degradation/oxidation of cell membrane constituents.

  • 3. Persson, P
    et al.
    Bergenståhl, B
    YKI – Ytkemiska institutet.
    Repulsive forces in lecithin glycol lamellar phases1985In: Biophysical Journal, ISSN 0006-3495, E-ISSN 1542-0086, Vol. 47, p. 743-746Article in journal (Refereed)
  • 4.
    Röding, Magnus
    et al.
    RISE - Research Institutes of Sweden, Bioscience and Materials, Agrifood and Bioscience.
    Lacroix, Leander
    RISE - Research Institutes of Sweden, Bioscience and Materials, Agrifood and Bioscience.
    Krona, Annika
    RISE - Research Institutes of Sweden, Bioscience and Materials, Agrifood and Bioscience.
    Gebäck, Tobias
    Chalmers University of Technology, Sweden.
    Loren, Niklas
    RISE - Research Institutes of Sweden, Bioscience and Materials, Agrifood and Bioscience. Chalmers University of Technology, Sweden.
    A Highly Accurate Pixel-Based FRAP Model Based on Spectral-Domain Numerical Methods2019In: Biophysical Journal, ISSN 0006-3495, E-ISSN 1542-0086, Vol. 116, no 7, p. 1348-1361Article in journal (Refereed)
    Abstract [en]

    We introduce a new, to our knowledge, numerical model based on spectral methods for analysis of fluorescence recovery after photobleaching data. The model covers pure diffusion and diffusion and binding (reaction-diffusion) with immobile binding sites, as well as arbitrary bleach region shapes. Fitting of the model is supported using both conventional recovery-curve-based estimation and pixel-based estimation, in which all individual pixels in the data are utilized. The model explicitly accounts for multiple bleach frames, diffusion (and binding) during bleaching, and bleaching during imaging. To our knowledge, no other fluorescence recovery after photobleaching framework incorporates all these model features and estimation methods. We thoroughly validate the model by comparison to stochastic simulations of particle dynamics and find it to be highly accurate. We perform simulation studies to compare recovery-curve-based estimation and pixel-based estimation in realistic settings and show that pixel-based estimation is the better method for parameter estimation as well as for distinguishing pure diffusion from diffusion and binding. We show that accounting for multiple bleach frames is important and that the effect of neglecting this is qualitatively different for the two estimation methods. We perform a simple experimental validation showing that pixel-based estimation provides better agreement with literature values than recovery-curve-based estimation and that accounting for multiple bleach frames improves the result. Further, the software developed in this work is freely available online.

  • 5.
    Schuster, Erich
    et al.
    RISE, SP – Sveriges Tekniska Forskningsinstitut, SP Sveriges tekniska forskningsinstitut, SIK – Institutet för livsmedel och bioteknik.
    Hermansson, Ann-Marie
    RISE, SP – Sveriges Tekniska Forskningsinstitut, SP Sveriges tekniska forskningsinstitut, SIK – Institutet för livsmedel och bioteknik.
    Öhgren, Camilla
    RISE, SP – Sveriges Tekniska Forskningsinstitut, SP Sveriges tekniska forskningsinstitut, SIK – Institutet för livsmedel och bioteknik.
    Rudemo, M.
    Loren, Niklas
    RISE, SP – Sveriges Tekniska Forskningsinstitut, SP Sveriges tekniska forskningsinstitut, SIK – Institutet för livsmedel och bioteknik.
    Interactions and diffusion in fine-stranded beta-lactoglobulin gels determined via FRAP and binding2014In: Biophysical Journal, ISSN 0006-3495, E-ISSN 1542-0086, Vol. 106, no 1, p. 253-262Article in journal (Refereed)
    Abstract [en]

    The effects of electrostatic interactions and obstruction by the microstructure on probe diffusion were determined in positively charged hydrogels. Probe diffusion in fine-stranded gels and solutions of ?-lactoglobulin at pH 3.5 was determined using fluorescence recovery after photobleaching (FRAP) and binding, which is widely used in biophysics. The microstructures of the ?-lactoglobulin gels were characterized using transmission electron microscopy. The effects of probe size and charge (negatively charged Na2-fluorescein (376Da) and weakly anionic 70kDa FITC-dextran), probe concentration (50 to 200 ppm), and ?-lactoglobulin concentration (9% to 12% w/w) on the diffusion properties and the electrostatic interaction between the negatively charged probes and the positively charged gels or solutions were evaluated. The results show that the diffusion of negatively charged Na2-fluorescein is strongly influenced by electrostatic interactions in the positively charged ?-lactoglobulin systems. A linear relationship between the pseudo-on binding rate constant and the ?-lactoglobulin concentration for three different probe concentrations was found. This validates an important assumption of existing biophysical FRAP and binding models, namely that the pseudo-on binding rate constant equals the product of the molecular binding rate constant and the concentration of the free binding sites. Indicators were established to clarify whether FRAP data should be analyzed using a binding-diffusion model or an obstruction-diffusion model. © 2014 by the Biophysical Society.

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