Change search
Refine search result
1 - 6 of 6
CiteExportLink to result list
Permanent link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Rows per page
  • 5
  • 10
  • 20
  • 50
  • 100
  • 250
Sort
  • Standard (Relevance)
  • Author A-Ö
  • Author Ö-A
  • Title A-Ö
  • Title Ö-A
  • Publication type A-Ö
  • Publication type Ö-A
  • Issued (Oldest first)
  • Issued (Newest first)
  • Created (Oldest first)
  • Created (Newest first)
  • Last updated (Oldest first)
  • Last updated (Newest first)
  • Disputation date (earliest first)
  • Disputation date (latest first)
  • Standard (Relevance)
  • Author A-Ö
  • Author Ö-A
  • Title A-Ö
  • Title Ö-A
  • Publication type A-Ö
  • Publication type Ö-A
  • Issued (Oldest first)
  • Issued (Newest first)
  • Created (Oldest first)
  • Created (Newest first)
  • Last updated (Oldest first)
  • Last updated (Newest first)
  • Disputation date (earliest first)
  • Disputation date (latest first)
Select
The maximal number of hits you can export is 250. When you want to export more records please use the Create feeds function.
  • 1.
    Carlred, Louise
    et al.
    RISE, SP – Sveriges Tekniska Forskningsinstitut, SP Kemi Material och Ytor, Medicinteknik. Chalmers University of Technology, Sweden.
    Vukojević, Vladana
    Karolinska Institute, Sweden.
    Johansson, Björn
    Karolinska Institute, Sweden.
    Schalling, Martin
    Karolinska Institute, Sweden.
    Höök, Fredrik
    Chalmers University of Technology, Sweden.
    Sjövall, Peter
    RISE, SP – Sveriges Tekniska Forskningsinstitut, SP Kemi Material och Ytor, Medicinteknik. Chalmers University of Technology, Sweden.
    Imaging of amyloid-β in alzheimer’s disease transgenic mouse brains with ToF-SIMS using immunoliposomes2016In: Biointerphases, ISSN 1934-8630, E-ISSN 1559-4106, Vol. 11, no 2, p. 1-11, article id 02A312Article in journal (Refereed)
    Abstract [en]

    Time-of-flight secondary ion mass spectrometry (ToF-SIMS) has been proven to successfully image different kinds of molecules, especially a variety of lipids, in biological samples. Proteins, however, are difficult to detect as specific entities with this method due to extensive fragmentation. To circumvent this issue, the authors present in this work a method developed for detection of proteins using antibody-conjugated liposomes, so called immunoliposomes, which are able to bind to the specific protein of interest. In combination with the capability of ToF-SIMS to detect native lipids in tissue samples, this method opens up the opportunity to analyze many different biomolecules, both lipids and proteins, at the same time, with high spatial resolution. The method has been applied to detect and image the distribution of amyloid-β (Aβ), a biologically relevant peptide in Alzheimer’s disease (AD), in transgenic mouse brain tissue. To ensure specific binding, the immunoliposome binding was verified on a model surface using quartz crystal microbalance with dissipation monitoring. The immunoliposome binding was also investigated on tissue sections with fluorescence microscopy, and compared with conventional immunohistochemistry using primary and secondary antibodies, demonstrating specific binding to Aβ. Using ToF-SIMS imaging, several endogenous lipids, such as cholesterol and sulfatides, were also detected in parallel with the immunoliposome-labeled Aβ deposits, which is an advantage compared to fluorescence microscopy. This method can thus potentially provide further information about lipid–protein interactions, which is important to understand the mechanisms of neurodegeneration in AD.

  • 2.
    Fromell, Karin
    et al.
    Uppsala University, Sweden.
    Yang, Yi
    University of Gothenburg, Sweden.
    Nilsson Ekdahl, Kristina
    Linnaeus University, Sweden.
    Nilsson, Bo
    Linnaeus University, Sweden.
    Berglin, Mattias
    RISE - Research Institutes of Sweden, Bioscience and Materials, Chemistry and Materials.
    Elwing, Hans
    University of Gothenburg, Sweden.
    Absence of conformational change in complement factor 3 and factor XII adsorbed to acrylate polymers is related to a high degree of polymer backbone flexibility2017In: Biointerphases, ISSN 1934-8630, E-ISSN 1559-4106, Vol. 12, no 2, article id 02D417Article in journal (Refereed)
    Abstract [en]

    In previous investigations, the authors have examined the adsorption of albumin, immunoglobulin, and fibrinogen to a series of acrylate polymers with different backbone and side-group flexibility. The authors showed that protein adsorption to acrylates with high flexibility, such as poly(lauryl methacrylate) (PLMA), tends to preserve native conformation. In the present study, the authors have continued this work by examining the conformational changes that occur during the binding of complement factor 3 (C3) and coagulation factor XII (FXII). Native C3 adsorbed readily to all solid surfaces tested, including a series of acrylate surfaces of varying backbone flexibility. However, a monoclonal antibody recognizing a "hidden" epitope of C3 (only exposed during C3 activation or denaturation) bound to the C3 on the rigid acrylate surfaces or on polystyrene (also rigid), but not to C3 on the flexible PLMA, indicating that varying degrees of conformational change had occurred with binding to different surfaces. Similarly, FXII was activated only on the rigid poly(butyl methacrylate) surface, as assessed by the formation of FXIIa-antithrombin (AT) complexes; in contrast, it remained in its native form on the flexible PLMA surface. The authors also found that water wettability hysteresis, defined as the difference between the advancing and receding contact angles, was highest for the PLMA surface, indicating that a dynamic change in the interface polymer structure may help protect the adsorbed protein from conformational changes and denaturation.

  • 3.
    Hannestad, Jonas
    et al.
    RISE - Research Institutes of Sweden, Bioscience and Materials, Chemistry and Materials. Chalmers University of Technology, Sweden.
    Höök, Fredrik
    Chalmers University of Technology, Sweden.
    Sjövall, Peter
    RISE - Research Institutes of Sweden, Bioscience and Materials, Chemistry and Materials. Chalmers University of Technology, Sweden.
    Nanometer-scale molecular organization in lipid membranes studied by time-of-flight secondary ion mass spectrometry2018In: Biointerphases, ISSN 1934-8630, E-ISSN 1559-4106, Vol. 13, no 3, article id 03B408Article in journal (Refereed)
    Abstract [en]

    The organization of lipid membranes plays an important role in a wide range of biological processes at different length scales. Herein, the authors present a procedure based on time-of-flight secondary ion mass spectrometry (ToF-SIMS) to characterize the nanometer-scale ordering of lipids in lipid membrane structures on surfaces. While ToF-SIMS is a powerful tool for label-free analysis of lipid-containing samples, its limited spatial resolution prevents in-depth knowledge of how lipid properties affect the molecular assembly of the membrane. The authors overcome this limitation by measuring the formation of lipid dimers, originating in the same nanometer-sized primary ion impact areas. The lipid dimers reflect the local lipid environment and thus allow us to characterize the membrane miscibility on the nanometer level. Using this technique, the authors show that the chemical properties of the constituting lipids are critical for the structure and organization of the membrane on both the nanometer and micrometer length scales. Our results show that even at lipid surface compositions favoring two-phase systems, lipids are still extracted from solid, gel phase, domains into the surrounding fluid supported lipid bilayer surrounding the gel phase domains. The technique offers a means to obtain detailed knowledge of the chemical composition and organization of lipid membranes with potential application in systems where labeling is not possible, such as cell-derived supported lipid bilayers.

    Download full text (pdf)
    fulltext
  • 4.
    Sun, Kangdi
    et al.
    University of Illinois at Urbana-Champaign, USA.
    Shoaib, Tooba
    Oak Ridge National Laboratory, USA.
    Rutland, Mark W.
    RISE Research Institutes of Sweden, Bioeconomy and Health, Material and Surface Design. KTH Royal Institute of Technology, Sweden; University of New South Wales, Australia; École Centrale de Lyon, France.
    Beller, Joseph
    University of Tennessee, USA.
    Do, Changwoo
    Oak Ridge National Laboratory, USA.
    Espinosa-Marzal, Rosa M
    University of Illinois at Urbana-Champaign, USA.
    Insight into the assembly of lipid-hyaluronan complexes in osteoarthritic conditions2023In: Biointerphases, ISSN 1934-8630, E-ISSN 1559-4106, Vol. 18, no 2, article id 021005Article in journal (Refereed)
    Abstract [en]

    Interactions between molecules in the synovial fluid and the cartilage surface may play a vital role in the formation of adsorbed films that contribute to the low friction of cartilage boundary lubrication. Osteoarthritis (OA) is the most common degenerative joint disease. Previous studies have shown that in OA-diseased joints, hyaluronan (HA) not only breaks down resulting in a much lower molecular weight (MW), but also its concentration is reduced ten times. Here, we have investigated the structural changes of lipid-HA complexes as a function of HA concentration and MW to simulate the physiologically relevant conditions that exist in healthy and diseased joints. Small angle neutron scattering and dynamic light scattering were used to determine the structure of HA-lipid vesicles in bulk solution, while a combination of atomic force microscopy and quartz crystal microbalance was applied to study their assembly on a gold surface. We infer a significant influence of both MW and HA concentrations on the structure of HA-lipid complexes in bulk and assembled on a gold surface. Our results suggest that low MW HA cannot form an amorphous layer on the gold surface, which is expected to negatively impact the mechanical integrity and longevity of the boundary layer and could contribute to the increased wear of the cartilage that has been reported in joints diseased with OA. © 2023 Author(s).

  • 5. Wigenius, J.A.
    et al.
    Fransson, S.
    RISE, SP – Sveriges Tekniska Forskningsinstitut, SP Sveriges tekniska forskningsinstitut, SIK – Institutet för livsmedel och bioteknik.
    von Post, F.
    Inganas, O.
    Protein biochips patterned by microcontact printing or by adsorption-soft lithography in two modes2008In: Biointerphases, ISSN 1934-8630, E-ISSN 1559-4106, Vol. 3, no 3, p. 75-82Article in journal (Refereed)
    Abstract [en]

    Patterning of proteins is critical to protein biochips. Printing of layers of proteins is well established, as is adsorption of proteins to surfaces properly modified with surface chemical functionalities. The authors show that simple methods based on soft lithography stamps can be used to prepare functional antibody chips through both these routes. Both methods incorporate transfer of the stamp material poly(dimethylsiloxane) (PDMS) to the biochip, whether intended or not intended. The results indicate that microcontact printing of proteins always includes PDMS transfer, thereby creating a possibility of unspecific adsorption to a hydrophobic domain. © 2008 American Vacuum Society.

  • 6.
    Wogelred, Louise
    et al.
    RISE - Research Institutes of Sweden, Bioscience and Materials, Chemistry and Materials. Chalmers University of Technology, Sweden.
    Höök, Fredrik
    Chalmers University of Technology, Sweden.
    Agnarsson, Björn
    Chalmers University of Technology, Sweden.
    Sjövall, Peter
    RISE - Research Institutes of Sweden, Bioscience and Materials, Chemistry and Materials. Chalmers University of Technology, Sweden.
    Toward multiplexed quantification of biomolecules on surfaces using time-of-flight secondary ion mass spectrometry2018In: Biointerphases, ISSN 1934-8630, E-ISSN 1559-4106, Vol. 13, no 3, article id 03B413Article in journal (Refereed)
    Abstract [en]

    Accurate detection and quantification of individual molecules is important for the development of improved diagnostic methods as well as biochemical characterization of disease progression and treatments. Time-of-flight secondary ion mass spectrometry (ToF-SIMS) is a surface analysis technique capable of imaging the distribution of specific molecules on surfaces with a high spatial resolution (<1 μm) and high sensitivity. ToF-SIMS is particularly suitable for detection of molecules up to ∼2 kDa, including lipids, whereas larger molecules, such as peptides and proteins, are fragmented during analysis, which makes them difficult to identify. In this study, an approach for extending the molecular detection capability of ToF-SIMS is presented, based on the specific binding of functionalized liposomes to molecular targets on the sample surface and subsequent detection of the liposomes by ToF-SIMS. Furthermore, by using different recognition elements conjugated to liposomes with different lipid compositions, simultaneous detection of different targets was accomplished. This multiplexing capability was investigated for two types of recognition elements (antibodies and cholera toxin) and for target molecules immobilized on surfaces using two frequently applied surface functionalization strategies: a supported lipid bilayer aimed to mimic a cell membrane and a polyethylene glycol modified surface, commonly employed in bioanalytical sensor applications. The efficacy of the conjugation protocols and the specificity of the recognition mechanism were confirmed using quartz crystal microbalance with dissipation monitoring, while fluorescence microscopy was used to validate the ToF-SIMS data and the reliability of the freeze-drying step required for ToF-SIMS analysis. The results demonstrated specific binding of the two types of liposomes to each target and showed a concentration-dependent binding to the targets on the different model surfaces. In particular, the possibility to use the contrasts in the mass spectra of SIMS to identify the concentration dependent coverage of different liposomes opens up new opportunities for multiplexed detection and quantification of molecules at biotechnology relevant interfaces.

1 - 6 of 6
CiteExportLink to result list
Permanent link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf