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  • 1.
    Bergström, Gunnar
    Linköping University, Department of Physics, Chemistry and Biology, Biotechnology. Linköping University, The Institute of Technology.
    Exploring the SPR methodology for monitoring of critical attributes in toxicity testing and bioproduction2012Licentiate thesis, comprehensive summary (Other academic)
    Abstract [en]

    Analysis of biological components is central in bioprocess monitoring, process control, product quality control and cell based toxicity assaying. One of these themes that is pursued in this thesis is the use of biosensors for monitoring of molecular markers, exploiting the natural selectivity of biomolecules. Another is the use of glycoconjugates to monitor the activity of biomolecules in a flu vaccine process is studied and were the sensor is based on the concept of weak affinity giving fast response time for the sensor.

    A third theme is monitoring of cell cultures used for toxicity testing different protein markers is of interest.

    When developing biosensor surfaces for new antigens commercial preparations of antibodies are often used. In this work we have chosen to look at lactate dehydrogenase (LDH) and describe the preparation and characterisation of antibody used in biosensor surface development.

    The design of a sensor surface is important for the characteristics of a sensor. By binding antibodies in an oriented manner to the surface a better control of the properties of the antibodies is achieved. The demonstrated method also has the advantage of in situ purification and provides a flexible platform for antibody evaluation and sensor development.

    In one sentence this thesis explores the possibility of utilizing recognition elements of a biosensor surface. In particular, surface plasmon resonance (SPR) is used as the primary biosensing tool, however most findings in are relevant for other biosensors.

    Moreover, the thesis approaches existing bioanalytical impediments, such as purity and accessibility of the recognition elements on the sensor surface and preparation strategies to achieve this.

    List of papers
    1. Monitoring of influenza virus hemagglutinin in process samples using weak affinity ligands and surface plasmon resonance
    Open this publication in new window or tab >>Monitoring of influenza virus hemagglutinin in process samples using weak affinity ligands and surface plasmon resonance
    Show others...
    2008 (English)In: Analytica Chimica Acta, ISSN 0003-2670, E-ISSN 1873-4324, Vol. 623, p. 66-75Article in journal (Refereed) Published
    Abstract [en]

    Surface plasmon resonance (SPR) was used to screen the interaction between a variety of affinity ligands and hemagglutinin (HA) from human influenza virus, with the aim of identifying low affinity ligands useful for the development of a rapid bioanalytical sensor. Three sialic acid-based structures and four lectins were evaluated as sensor ligands. The sialic acid-based ligands included a natural sialic acid-containing glycoprotein, human α1-acid glycoprotein (α1-AGP), and two synthetic 6′-sialyllactose-conjugates, with varying degree of substitution. The interaction of HA with the four lectin-based ligands, concanavalin A (Con A), wheat germ agglutinin (WGA), Maackia amurensis lectin (MAL), and Sambucus nigra agglutinin (SNA), showed a wide variation of affinity strengths. Affinity and kinetics data were estimated. Strong affinities were observed for Con A, WGA, α1-AGP, and a 6′-sialyllactose-conjugate with a high substitution degree, and low affinities were observed for MAL and a 6′-sialyllactose-conjugate with low substitution.

    The main objective, to identify a low affinity ligand which could be used for on-line monitoring and product quantification, was met by a 6′-sialyllactose–ovalbumin conjugate that had 0.6 mol ligand per mol carrier protein. The apparent affinity of this ligand was estimated to be 1.5 ± 0.03 μM (KD) on the SPR surface. Vaccine process samples containing HA were analyzed in the range 10–100 μg HA mL−1 and correlated with single-radial immunodiffusion. The coefficient of variation on the same chip was between 0.010 and 0.091.

    Place, publisher, year, edition, pages
    Elsevier, 2008
    Keywords
    Influenza virus hemagglutinin; Affinity ligand; Surface plasmon resonance; Low affinity; Weak affinity
    National Category
    Natural Sciences
    Identifiers
    urn:nbn:se:liu:diva-44210 (URN)10.1016/j.aca.2008.06.005 (DOI)76040 (Local ID)76040 (Archive number)76040 (OAI)
    Available from: 2009-10-10 Created: 2009-10-10 Last updated: 2019-01-22Bibliographically approved
    2. Initial development towards in vitro toxicity assay for lactate dehydrogenase using surface plasmon resonance
    Open this publication in new window or tab >>Initial development towards in vitro toxicity assay for lactate dehydrogenase using surface plasmon resonance
    (English)Manuscript (preprint) (Other academic)
    Abstract [en]

    Work with initial development towards in vitro toxicity assay for lactate dehydrogenase (LDH) using surface plasmon resonance is described. LDH is one of the important versatile biomarkers in in vitro hepatotoxicity. In this report LDH is detected by surface plasmon resonance using antibodies directly immobilized to the sensor surface. The assay is further extended with protein G immobilized to the surface to capture the antibody ligand. This has the advantage of simultaneously and on site purify and orient antibody ligand.

    Keywords
    Lactate dehydrogenase, surface plasmon resonance, in vitro toxicity, biosensor, protein G
    National Category
    Natural Sciences
    Identifiers
    urn:nbn:se:liu:diva-73409 (URN)
    Available from: 2012-01-03 Created: 2012-01-03 Last updated: 2019-01-22Bibliographically approved
    3. Orientation and capturing of antibody affinity ligands: Applications to surface plasmon resonance biochips
    Open this publication in new window or tab >>Orientation and capturing of antibody affinity ligands: Applications to surface plasmon resonance biochips
    2011 (English)In: Sensors and actuators. B, Chemical, ISSN 0925-4005, E-ISSN 1873-3077, Vol. 158, no 1, p. 265-270Article in journal (Refereed) Published
    Abstract [en]

    A surface plasmon resonance (SPR) sensor chip with immobilized protein G was used for simultaneously capturing, purifying and orienting antibody ligands. The ligands were further stabilized by chemical cross-linking. This procedure of designing the sensor chip improved efficient use of the ligands and could prolong the analytical use. less thanbrgreater than less thanbrgreater thanThe procedure was evaluated on standard dextran-coated sensor chips onto which commercial semi-purified antibodies towards human serum albumin and human troponin where captured and used for analysing their antigens. less thanbrgreater than less thanbrgreater thanThe procedure demonstrates a general design approach for presenting the biorecognition element on a biosensor surface which enhances sensitivity, stability and selectivity at the same time as an impure ligand is purified.

    Place, publisher, year, edition, pages
    Elsevier, 2011
    Keywords
    Biosensor, Affinity interaction, SPR, Biacore, Protein G, Sensor chip
    National Category
    Engineering and Technology
    Identifiers
    urn:nbn:se:liu:diva-71770 (URN)10.1016/j.snb.2011.06.017 (DOI)000295500200037 ()
    Note

    Funding Agencies|European Commission|LSHB-CT-2007-037636|

    Available from: 2011-11-04 Created: 2011-11-04 Last updated: 2019-01-22
  • 2.
    Bergström, Gunnar
    Linköping University, Department of Physics, Chemistry and Biology, Biotechnology. Linköping University, Faculty of Science & Engineering.
    Microfluidic biosensor systems for cardiotoxicity assaying2015Doctoral thesis, comprehensive summary (Other academic)
    Abstract [en]

    Toxicity screening is an important part of pharmaceutical development and early detection of toxic side effects provide the opportunity for early redesign or termination of unfeasible projects. Today toxicity testing is relying on experiments on animals. Ethical concerns, high costs and problems with interspecies variability in animal experiments have introduced incentives for cell-based toxicity assays. The recent development of stem cell technology have raised the hope for toxicity testing with higher predictivity that can reduce the amount of animals sacrificed, increase the patient safety and reduce the costs in pharmaceutical development.

    Cell development and behavior is to a large extent dependent on the microenvironment. Microfluidic techniques can be used to build small-sized structures that provide the opportunity to introduce a high degree of control of the cell culture environment with features in cell sizes. In this thesis is demonstrated two different methods for infusing cells into microfluidic cell culture devices using either cells clustered in cardiac bodies during differentiation or cells pre-seeded in microporous carriers prior to infusion.

    Microfluidic cell culture devices are well suited for optical  evaluation. Demonstrated in this thesis is fluorescent staining in combination with confocal microscopy as well as automated imaging with evaluation of beating frequency of cardiomyocyte cell clusters can be used to assess toxicity of cells cultured in microfluidic devices.

    Biosensors use biological recognition elements to measure the presence of a chemical substance, for example low concentrations of biomarkers secreted by cells in a toxicity assay. Especially capacitive biosensors have shown very low limit of detection. In addition, protein G is demonstrated as an affinity ligand to capture IgG antibodies used as recognition element in a biosensor application or used for antibody screening.

    List of papers
    1. Orientation and capturing of antibody affinity ligands: Applications to surface plasmon resonance biochips
    Open this publication in new window or tab >>Orientation and capturing of antibody affinity ligands: Applications to surface plasmon resonance biochips
    2011 (English)In: Sensors and actuators. B, Chemical, ISSN 0925-4005, E-ISSN 1873-3077, Vol. 158, no 1, p. 265-270Article in journal (Refereed) Published
    Abstract [en]

    A surface plasmon resonance (SPR) sensor chip with immobilized protein G was used for simultaneously capturing, purifying and orienting antibody ligands. The ligands were further stabilized by chemical cross-linking. This procedure of designing the sensor chip improved efficient use of the ligands and could prolong the analytical use. less thanbrgreater than less thanbrgreater thanThe procedure was evaluated on standard dextran-coated sensor chips onto which commercial semi-purified antibodies towards human serum albumin and human troponin where captured and used for analysing their antigens. less thanbrgreater than less thanbrgreater thanThe procedure demonstrates a general design approach for presenting the biorecognition element on a biosensor surface which enhances sensitivity, stability and selectivity at the same time as an impure ligand is purified.

    Place, publisher, year, edition, pages
    Elsevier, 2011
    Keywords
    Biosensor, Affinity interaction, SPR, Biacore, Protein G, Sensor chip
    National Category
    Engineering and Technology
    Identifiers
    urn:nbn:se:liu:diva-71770 (URN)10.1016/j.snb.2011.06.017 (DOI)000295500200037 ()
    Note

    Funding Agencies|European Commission|LSHB-CT-2007-037636|

    Available from: 2011-11-04 Created: 2011-11-04 Last updated: 2019-01-22
    2. Macroporous microcarriers for introducing cells into a microfluidic chip
    Open this publication in new window or tab >>Macroporous microcarriers for introducing cells into a microfluidic chip
    2014 (English)In: Lab on a Chip, ISSN 1473-0197, E-ISSN 1473-0189, Vol. 14, no 18, p. 3502-3504Article in journal (Refereed) Published
    Abstract [en]

    Macroporous gelatin beads (CultiSpher™ microcarriers) provide a convenient method for rapidly and reliably introducing cells cultured ex situ into a microfluidic device, where the spheres create a 3D environment for continued cell proliferation. We demonstrate the usefulness of this technique with a proof-of-concept viability analysis of cardiac cells after treatment with doxorubicin. © 2014 the Partner Organisations.

    Place, publisher, year, edition, pages
    Royal Society of Chemistry, 2014
    National Category
    Biological Sciences Physical Sciences
    Identifiers
    urn:nbn:se:liu:diva-109971 (URN)10.1039/c4lc00693c (DOI)000340474300008 ()25068539 (PubMedID)2-s2.0-84905837163 (Scopus ID)
    Funder
    Swedish Research Council, 2008-7537 2011-6404
    Note

    Acknowledgements

    The primary embryonic cardiomyocytes were provided byJordi Altimiras, Department of Physics, Chemistry andBiology, Linköping University. The authors thank the SwedishResearch Council (Vetenskapsrådet) for fundingviagrants 2008-7537 and 2011-6404

    Available from: 2014-08-29 Created: 2014-08-29 Last updated: 2019-01-22Bibliographically approved
    3. Capacitive biosensor for detection of toxicity biomarkers
    Open this publication in new window or tab >>Capacitive biosensor for detection of toxicity biomarkers
    2015 (English)Manuscript (preprint) (Other academic)
    Abstract [en]

    Microfluidic devices are rapidly gaining importance for in vitro toxicity testing. Biomarker detection in microfluidic assays are however challenging due to small sample sizes and low analyte concentration. Capacitive electrochemical biosensors have been reported to have high sensitivity and properties that are amenable for implementation into microfluidic devices.

    In this work a biosensor application for troponin T (TnT) is presented. The sensor showed linear response to analyte over five orders of magnitude with the lowest detectable signal at 10-13 M. The sensor proved to be able to detect TnT spiked in cell culture media at concentrations relevant for cell cultures.

    National Category
    Biological Sciences Physical Sciences
    Identifiers
    urn:nbn:se:liu:diva-118293 (URN)
    Available from: 2015-05-26 Created: 2015-05-26 Last updated: 2019-01-22
    4. Stem cell derived in vivo-like human cardiac bodies in a microfluidic device for toxicity testing by beating frequency imaging
    Open this publication in new window or tab >>Stem cell derived in vivo-like human cardiac bodies in a microfluidic device for toxicity testing by beating frequency imaging
    Show others...
    2015 (English)In: Lab on a Chip, ISSN 1473-0197, E-ISSN 1473-0189, Vol. 15, no 15, p. 3242-3249Article in journal (Refereed) Published
    Abstract [en]

    Beating in vivo-like human cardiac bodies (CBs) were used in a microfluidic device for testing cardiotoxicity. The CBs, cardiomyocyte cell clusters derived from induced pluripotent stem cells, exhibited typical structural and functional properties of the native human myocardium. The CBs were captured in niches along a perfusion channel in the device. Video imaging was utilized for automatic monitoring of the beating frequency of each individual CB. The device allowed assessment of cardiotoxic effects on the 3D clustered cardiomyocytes from the drug substances doxorubicin, verapamil and quinidine. Beating frequency data recorded over a period of 6 hours are presented and compared to literature data. The results indicate that this microfluidic setup with imaging of CB characteristics provides a new opportunity for label-free, non-invasive investigation of toxic effects in a 3D microenvironment.

    Place, publisher, year, edition, pages
    Royal Society of Chemistry, 2015
    National Category
    Biological Sciences Physical Sciences
    Identifiers
    urn:nbn:se:liu:diva-118294 (URN)10.1039/c5lc00449g (DOI)000358022900017 ()
    Available from: 2015-05-26 Created: 2015-05-26 Last updated: 2019-01-22Bibliographically approved
  • 3.
    Bergström, Gunnar
    et al.
    Linköping University, Department of Physics, Chemistry and Biology, Biotechnology. Linköping University, The Institute of Technology.
    Christoffersson, Jonas
    Linköping University, Department of Physics, Chemistry and Biology, Biotechnology. Linköping University, Faculty of Science & Engineering.
    Schwanke, Kristin
    Hannover Medical School, Leibniz Research Laboratories for Biotechnology and Artificial Organs -LEBAO-, Hannover, Germany.
    Zweigerdt, Robert
    Hannover Medical School, Leibniz Research Laboratories for Biotechnology and Artificial Organs -LEBAO-, Hannover, Germany.
    Mandenius, Carl-Fredrik
    Linköping University, Department of Physics, Chemistry and Biology, Biotechnology. Linköping University, The Institute of Technology.
    Stem cell derived in vivo-like human cardiac bodies in a microfluidic device for toxicity testing by beating frequency imaging2015In: Lab on a Chip, ISSN 1473-0197, E-ISSN 1473-0189, Vol. 15, no 15, p. 3242-3249Article in journal (Refereed)
    Abstract [en]

    Beating in vivo-like human cardiac bodies (CBs) were used in a microfluidic device for testing cardiotoxicity. The CBs, cardiomyocyte cell clusters derived from induced pluripotent stem cells, exhibited typical structural and functional properties of the native human myocardium. The CBs were captured in niches along a perfusion channel in the device. Video imaging was utilized for automatic monitoring of the beating frequency of each individual CB. The device allowed assessment of cardiotoxic effects on the 3D clustered cardiomyocytes from the drug substances doxorubicin, verapamil and quinidine. Beating frequency data recorded over a period of 6 hours are presented and compared to literature data. The results indicate that this microfluidic setup with imaging of CB characteristics provides a new opportunity for label-free, non-invasive investigation of toxic effects in a 3D microenvironment.

  • 4.
    Bergström, Gunnar
    et al.
    Linköping University, Department of Physics, Chemistry and Biology, Biotechnology. Linköping University, The Institute of Technology.
    Kuusk, Ave
    Linköping University, Department of Physics, Chemistry and Biology. Linköping University, Faculty of Science & Engineering.
    Mandenius, Carl-Fredrik
    Linköping University, Department of Physics, Chemistry and Biology, Biotechnology. Linköping University, The Institute of Technology.
    Capacitive biosensor for detection of toxicity biomarkers2015Manuscript (preprint) (Other academic)
    Abstract [en]

    Microfluidic devices are rapidly gaining importance for in vitro toxicity testing. Biomarker detection in microfluidic assays are however challenging due to small sample sizes and low analyte concentration. Capacitive electrochemical biosensors have been reported to have high sensitivity and properties that are amenable for implementation into microfluidic devices.

    In this work a biosensor application for troponin T (TnT) is presented. The sensor showed linear response to analyte over five orders of magnitude with the lowest detectable signal at 10-13 M. The sensor proved to be able to detect TnT spiked in cell culture media at concentrations relevant for cell cultures.

  • 5.
    Bergström, Gunnar
    et al.
    Linköping University, Department of Physics, Chemistry and Biology, Biotechnology. Linköping University, The Institute of Technology.
    Mandenius, Carl-Fredrik
    Linköping University, Department of Physics, Chemistry and Biology, Biotechnology. Linköping University, The Institute of Technology.
    Initial development towards in vitro toxicity assay for lactate dehydrogenase using surface plasmon resonanceManuscript (preprint) (Other academic)
    Abstract [en]

    Work with initial development towards in vitro toxicity assay for lactate dehydrogenase (LDH) using surface plasmon resonance is described. LDH is one of the important versatile biomarkers in in vitro hepatotoxicity. In this report LDH is detected by surface plasmon resonance using antibodies directly immobilized to the sensor surface. The assay is further extended with protein G immobilized to the surface to capture the antibody ligand. This has the advantage of simultaneously and on site purify and orient antibody ligand.

  • 6.
    Bergström, Gunnar
    et al.
    Linköping University, Department of Physics, Chemistry and Biology, Biotechnology. Linköping University, Faculty of Science & Engineering.
    Mandenius, Carl-Fredrik
    Linköping University, Department of Physics, Chemistry and Biology, Biotechnology. Linköping University, The Institute of Technology.
    Orientation and capturing of antibody affinity ligands: Applications to surface plasmon resonance biochips2011In: Sensors and actuators. B, Chemical, ISSN 0925-4005, E-ISSN 1873-3077, Vol. 158, no 1, p. 265-270Article in journal (Refereed)
    Abstract [en]

    A surface plasmon resonance (SPR) sensor chip with immobilized protein G was used for simultaneously capturing, purifying and orienting antibody ligands. The ligands were further stabilized by chemical cross-linking. This procedure of designing the sensor chip improved efficient use of the ligands and could prolong the analytical use. less thanbrgreater than less thanbrgreater thanThe procedure was evaluated on standard dextran-coated sensor chips onto which commercial semi-purified antibodies towards human serum albumin and human troponin where captured and used for analysing their antigens. less thanbrgreater than less thanbrgreater thanThe procedure demonstrates a general design approach for presenting the biorecognition element on a biosensor surface which enhances sensitivity, stability and selectivity at the same time as an impure ligand is purified.

  • 7.
    Bergström, Gunnar
    et al.
    Linköping University, Department of Physics, Chemistry and Biology, Biotechnology. Linköping University, The Institute of Technology.
    Nilsson, K.
    Percell Biolytica AB, Åstorp, Sweden.
    Mandenius, Carl-Fredrik
    Linköping University, Department of Physics, Chemistry and Biology, Biotechnology. Linköping University, The Institute of Technology.
    Robinson, Nathaniel D
    Linköping University, Department of Physics, Chemistry and Biology, Surface Physics and Chemistry. Linköping University, The Institute of Technology.
    Macroporous microcarriers for introducing cells into a microfluidic chip2014In: Lab on a Chip, ISSN 1473-0197, E-ISSN 1473-0189, Vol. 14, no 18, p. 3502-3504Article in journal (Refereed)
    Abstract [en]

    Macroporous gelatin beads (CultiSpher™ microcarriers) provide a convenient method for rapidly and reliably introducing cells cultured ex situ into a microfluidic device, where the spheres create a 3D environment for continued cell proliferation. We demonstrate the usefulness of this technique with a proof-of-concept viability analysis of cardiac cells after treatment with doxorubicin. © 2014 the Partner Organisations.

  • 8.
    Duong-Thi, Minh-Dao
    et al.
    Linnaeus Univ, Dept Chem & Biomed Sci, SE-39182 Kalmar, Sweden.
    Bergström, Gunnar
    Linköping University, Department of Physics, Chemistry and Biology, Biotechnology. Linköping University, The Institute of Technology.
    Mandenius, Carl-Fredrik
    Linköping University, Department of Physics, Chemistry and Biology, Biotechnology. Linköping University, The Institute of Technology.
    Bergstrom, Maria
    Linnaeus University, Sweden .
    Fex, Tomas
    University of Gothenburg, Sweden .
    Ohlson, Sten
    Nanyang Technology University, Singapore .
    Comparison of weak affinity chromatography and surface plasmon resonance in determining affinity of small molecules2014In: Analytical Biochemistry, ISSN 0003-2697, E-ISSN 1096-0309, Vol. 461, p. 57-59Article in journal (Refereed)
    Abstract [en]

    In this study, we compared affinity data from surface plasmon resonance (SPR) and weak affinity chromatography (WAC), two established techniques for determination of weak affinity (mM-mu M) small molecule-protein interactions. In the current comparison, thrombin was used as target protein. In WAC the affinity constant (K-D) was determined from retention times, and in SPR it was determined by Langmuir isotherm fitting of steady-state responses. Results indicate a strong correlation between the two methods (R-2 = 0.995, P less than 0.0001).

  • 9.
    Ekblad, Tobias
    et al.
    Linköping University, The Institute of Technology. Linköping University, Department of Physics, Chemistry and Biology, Sensor Science and Molecular Physics .
    Bergström, Gunnar
    Linköping University, The Institute of Technology. Linköping University, Department of Physics, Chemistry and Biology, Biotechnology .
    Ederth, Thomas
    Linköping University, The Institute of Technology. Linköping University, Department of Physics, Chemistry and Biology, Sensor Science and Molecular Physics .
    Conlan, Sheelagh L.
    Liu, Yunli
    Zhao, Qi
    DSouza, Fraddry
    Donnelly, GlenT.
    Willemsen, Peter R.
    Pettitt, Michala E.
    Callow, Maureen E.
    Callow, James A.
    Liedberg, Bo
    Linköping University, The Institute of Technology. Linköping University, Department of Physics, Chemistry and Biology, Sensor Science and Molecular Physics .
    Poly(ethylene glycol)-Containing Hydrogel Surfaces for Antifouling Applications in Marine and Freshwater Environments2008In: Biomacromolecules, ISSN 1525-7797, E-ISSN 1526-4602, Vol. 9, no 10, p. 2775-2783Article in journal (Refereed)
    Abstract [en]

       

  • 10.
    Johansson, Leif B. G.
    et al.
    Linköping University, Department of Physics, Chemistry and Biology, Chemistry. Linköping University, The Institute of Technology.
    Simon, Rozalyn
    Linköping University, Department of Physics, Chemistry and Biology, Chemistry. Linköping University, The Institute of Technology.
    Bergström, Gunnar
    Linköping University, Department of Physics, Chemistry and Biology, Biotechnology. Linköping University, The Institute of Technology.
    Eriksson, Mikaela
    Linköping University, Department of Physics, Chemistry and Biology, Chemistry. Linköping University, The Institute of Technology.
    Prokop, Stefan
    Charite, Germany.
    Mandenius, Carl-Fredrik
    Linköping University, Department of Physics, Chemistry and Biology, Biotechnology. Linköping University, The Institute of Technology.
    Heppner, Frank L.
    Charite, Germany.
    Åslund, Andreas
    Linköping University, Department of Physics, Chemistry and Biology, Chemistry. Linköping University, The Institute of Technology.
    Nilsson, Peter
    Linköping University, Department of Physics, Chemistry and Biology, Chemistry. Linköping University, The Institute of Technology.
    An azide functionalized oligothiophene ligand - A versatile tool for multimodal detection of disease associated protein aggregates2015In: Biosensors & bioelectronics, ISSN 0956-5663, E-ISSN 1873-4235, Vol. 63, p. 204-211Article in journal (Refereed)
    Abstract [en]

    Ligands for identifying protein aggregates are of great interest as such deposits are the pathological hallmark of a wide range of severe diseases including Alzheimers and Parkinsons disease. Here we report the synthesis of an azide functionalized fluorescent pentameric oligothiophene that can be utilized as a ligand for multimodal detection of disease-associated protein aggregates. The azide functionalization allows for attachment of the ligand to a surface by conventional click chemistry without disturbing selective interaction with protein aggregates and the oligothiophene-aggregate interaction can be detected by fluorescence or surface plasmon resonance. In addition, a methodology where the oligothiophene ligand is employed as a capturing molecule selective for aggregated proteins in combination with an antibody detecting a distinct peptide/protein is also presented. We foresee that this methodology will offer the possibility to create a variety of multiplex sensing systems for sensitive and selective detection of protein aggregates, the pathological hallmarks of several neurodegenerative diseases.

  • 11.
    Mandenius, Carl-Fredrik
    et al.
    Linköping University, Department of Physics, Chemistry and Biology, Biotechnology. Linköping University, The Institute of Technology.
    Wang, Ronghui
    Linköping University, Department of Physics, Chemistry and Biology. Linköping University, The Institute of Technology.
    Aldén, Anna
    School of Pure and Applied Natural Sciences, University of Kalmar, SE-391 82 Kalmar, Sweden.
    Bergström, Gunnar
    Linköping University, Department of Physics, Chemistry and Biology. Linköping University, The Institute of Technology.
    Thébault, Sabine
    Process Development Purification, Sanofi Pasteur, Campus Merieux 1541, Avenue Marcel Merieux, F-69280 Marcy l’ Etoile, France.
    Lutsch, Charles
    Process Development Purification, Sanofi Pasteur, Campus Merieux 1541, Avenue Marcel Merieux, F-69280 Marcy l’ Etoile, France.
    Ohlson, Sten
    School of Pure and Applied Natural Sciences, University of Kalmar, SE-391 82 Kalmar, Sweden.
    Monitoring of influenza virus hemagglutinin in process samples using weak affinity ligands and surface plasmon resonance2008In: Analytica Chimica Acta, ISSN 0003-2670, E-ISSN 1873-4324, Vol. 623, p. 66-75Article in journal (Refereed)
    Abstract [en]

    Surface plasmon resonance (SPR) was used to screen the interaction between a variety of affinity ligands and hemagglutinin (HA) from human influenza virus, with the aim of identifying low affinity ligands useful for the development of a rapid bioanalytical sensor. Three sialic acid-based structures and four lectins were evaluated as sensor ligands. The sialic acid-based ligands included a natural sialic acid-containing glycoprotein, human α1-acid glycoprotein (α1-AGP), and two synthetic 6′-sialyllactose-conjugates, with varying degree of substitution. The interaction of HA with the four lectin-based ligands, concanavalin A (Con A), wheat germ agglutinin (WGA), Maackia amurensis lectin (MAL), and Sambucus nigra agglutinin (SNA), showed a wide variation of affinity strengths. Affinity and kinetics data were estimated. Strong affinities were observed for Con A, WGA, α1-AGP, and a 6′-sialyllactose-conjugate with a high substitution degree, and low affinities were observed for MAL and a 6′-sialyllactose-conjugate with low substitution.

    The main objective, to identify a low affinity ligand which could be used for on-line monitoring and product quantification, was met by a 6′-sialyllactose–ovalbumin conjugate that had 0.6 mol ligand per mol carrier protein. The apparent affinity of this ligand was estimated to be 1.5 ± 0.03 μM (KD) on the SPR surface. Vaccine process samples containing HA were analyzed in the range 10–100 μg HA mL−1 and correlated with single-radial immunodiffusion. The coefficient of variation on the same chip was between 0.010 and 0.091.

  • 12.
    Wickham, Abeni
    et al.
    Linköping University, Department of Physics, Chemistry and Biology, Molecular Physics. Linköping University, Faculty of Science & Engineering.
    Sjölander, Daniel
    Linköping University, Department of Physics, Chemistry and Biology. Linköping University, Faculty of Science & Engineering.
    Bergström, Gunnar
    Linköping University, Department of Physics, Chemistry and Biology, Biotechnology. Linköping University, Faculty of Science & Engineering.
    Wang, Ergang
    Chalmers, Sweden.
    Rajendran, Vijayalakshmi
    Linköping University, Department of Clinical and Experimental Medicine, Division of Cell Biology. Linköping University, Faculty of Health Sciences.
    Hildesjö, Camilla
    Linköping University, Department of Clinical and Experimental Medicine, Division of Clinical Sciences. Linköping University, Faculty of Medicine and Health Sciences.
    Skoglund, Karin
    Linköping University, Department of Clinical and Experimental Medicine, Division of Neuro and Inflammation Science. Linköping University, Faculty of Medicine and Health Sciences.
    Nilsson, Peter
    Linköping University, Department of Physics, Chemistry and Biology, Chemistry. Linköping University, Faculty of Science & Engineering.
    Aili, Daniel
    Linköping University, Department of Physics, Chemistry and Biology, Molecular Physics. Linköping University, Faculty of Science & Engineering.
    Near-Infrared Emitting and Pro-Angiogenic Electrospun Conjugated Polymer Scaffold for Optical Biomaterial Tracking2015In: Advanced Functional Materials, ISSN 1616-301X, E-ISSN 1616-3028, Vol. 25, no 27, p. 4274-4281Article in journal (Refereed)
    Abstract [en]

    Noninvasive tracking of biomaterials is vital for determining the fate and degradation of an implant in vivo, and to show its role in tissue regeneration. Current biomaterials have no inherent capacity to enable tracing but require labeling with, for example, fluorescent dyes, or nanoparticles. Here a novel biocompatible fully conjugated electrospun scaffold is described, based on a semiconducting luminescent polymer that can be visualized in situ after implantation using fluorescence imaging. The polymer, poly [2,3-bis-(3-octyloxyphenyl)quinoxaline-5,8-diyl-alt -thiophene-2,5-diyl] (TQ1), is electrospun to form a fibrous mat. The fibers display fluorescence emission in the near-infrared region with lifetimes in the sub-nanosecond range, optimal for in situ imaging. The material shows no cytotoxic behaviors for embryonic chicken cardiomyocytes and mouse myoblasts, and cells migrate onto the TQ1 fibers even in the presence of a collagen substrate. Subcutaneous implantations of the material in rats show incorporation of the TQ1 fibers within the tissue, with limited inflammation and a preponderance of small capillaries around the fibers. The fluorescent properties of the TQ1 fibers are fully retained for up to 90 d following implantation and they can be clearly visualized in tissue using fluorescence and lifetime imaging, thus making it both a pro-angiogenic and traceable biomaterial.

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