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  • 1.
    Andersson, Jens
    et al.
    Linköping University, The Institute of Technology. Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics .
    Björk, Per
    Linköping University, The Institute of Technology. Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics .
    Herland, Anna
    Linköping University, The Institute of Technology. Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics .
    Tvingstedt, Kristofer
    Linköping University, The Institute of Technology. Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics .
    Inganäs, Olle
    Linköping University, The Institute of Technology. Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics .
    Biomolecules and conjugated polyelectrolytes in patterning2006In: NaPa spring meeting 06 Köpenhamn,2006, 2006Conference paper (Other academic)
  • 2.
    Andersson, Jens
    et al.
    Linköping University, The Institute of Technology. Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics .
    Åsberg, Peter
    Linköping University, The Institute of Technology. Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics .
    Herland, Anna
    Linköping University, The Institute of Technology. Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics .
    Fransson, Sophia
    Linköping University, The Institute of Technology. Linköping University, Department of Physics, Chemistry and Biology.
    von Post, Fredrik
    Linköping University, The Institute of Technology. Linköping University, Department of Physics, Chemistry and Biology.
    Inganäs, Olle
    Linköping University, The Institute of Technology. Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics .
    Conjugated polyelectrolytes as reporter molecules; biochip constructed by Soft litography methods2006In: ICSM summer 06 Dublin,2006, 2006Conference paper (Other academic)
    Abstract [en]

       

  • 3.
    Andersson, Viktor
    et al.
    Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics. Linköping University, The Institute of Technology.
    Herland, Anna
    Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics. Linköping University, The Institute of Technology.
    Masich, Sergej
    Karolinska Institutet.
    Inganäs, Olle
    Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics. Linköping University, The Institute of Technology.
    Imaging of the 3D Nanostructure of a Polymer Solar Cell by Electron Tomography2009In: Nano letters (Print), ISSN 1530-6984, E-ISSN 1530-6992, Vol. 9, no 2, p. 853-855Article in journal (Refereed)
    Abstract [en]

    Electron tomography has been used for analyzing the active layer in a polymer solar cell, a bulk heterojunction of an alternating copolymer of fluorene and a derivative of fullerene. The method supplies a three-dimensional representation of the morphology of the film, where domains with different scattering properties may be distinguished. The reconstruction shows good contrast between the two phases included in the film and demonstrates that electron tomography is an adequate tool for investigations of the three-dimensional nanostructure of the amorphous materials used in polymer solar cells.

  • 4.
    Barrau, Sophie
    et al.
    Linköping University, The Institute of Technology. Linköping University, Department of Physics, Chemistry and Biology.
    Zhang, Fengling
    Linköping University, The Institute of Technology. Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics .
    Herland, Anna
    Linköping University, The Institute of Technology. Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics .
    Mammo, W.
    Chalmers University of Technology.
    Andersson, Mats R.
    Chalmers University of Technology.
    Inganäs, Olle
    Linköping University, The Institute of Technology. Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics .
    Integration of Amyloid Nanowires in Organic Solar Cells2008In: Applied Physics Letters, ISSN 0003-6951, E-ISSN 1077-3118, Vol. 93, p. 23307-Article in journal (Refereed)
    Abstract [en]

      

  • 5.
    Björk, Per
    et al.
    Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics . Linköping University, The Institute of Technology.
    Herland, Anna
    Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics . Linköping University, The Institute of Technology.
    Hamedi, Mahiar
    Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics . Linköping University, The Institute of Technology.
    Inganäs, Olle
    Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics . Linköping University, The Institute of Technology.
    Biomolecular nanowires decorated by organic electronic polymers2010In: JOURNAL OF MATERIALS CHEMISTRY, ISSN 0959-9428, Vol. 20, no 12, p. 2269-2276Article in journal (Refereed)
    Abstract [en]

    We demonstrate the shaping and forming of organic electronic polymers into designer nanostructures using biomacromolecules. In order to create nanowires, nanohelixes and assemblies of these, we coordinate semiconducting or metallic polymers to biomolecular polymers in the form of DNA and misfolded proteins. Optoelectronic and electrochemical devices utilizing these shaped materials are discussed.

  • 6.
    Björk, Per
    et al.
    Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics . Linköping University, The Institute of Technology.
    Herland, Anna
    Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics . Linköping University, The Institute of Technology.
    Scheblykin, Ivan
    Department of Chemical.
    Inganäs, Olle
    Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics . Linköping University, The Institute of Technology.
    Single molecular imaging and spectroscopy of conjugated polyelectrolytes decorated on stretched aligned DNA2005In: Nano Letters, ISSN 1530-6984, Vol. 5, no 10, p. 1948-1953Article in journal (Refereed)
    Abstract [en]

    DNA is the prototype template for building nanoelectronic devices by self-assembly. The electronic functions are made possible by coordinating electronic polymer chains to DNA. This paper demonstrates two methods for fabrication of aligned and ordered DNA nanowires complexed with conjugated polyelectrolytes (CPEs). The complex can be formed either in solution prior to stretching or after stretching of the bare DNA on a surface. Molecular combing was used to stretch the complexes on surface energy patterned surfaces, and PMMA for the bare DNA. Single molecular spectroscopy, in fluorescence, and microscopy, in atomic force microscopy, give evidence for coordination of the short CPE chains to the aligned DNA.

  • 7.
    Hamedi, Mahiar
    et al.
    Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics . Linköping University, The Institute of Technology.
    Herland, Anna
    Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics . Linköping University, The Institute of Technology.
    Karlsson, Roger H
    Linköping University, Department of Physics, Chemistry and Biology. Linköping University, The Institute of Technology.
    Inganäs, Olle
    Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics . Linköping University, The Institute of Technology.
    Electrochemical Devices Made from Conducting Nanowire Networks Self-Assembled from Amyloid Fibrils and Alkoxysulfonate PEDOT2008In: Nano letters (Print), ISSN 1530-6984, E-ISSN 1530-6992, Vol. 8, no 6, p. 1736-1740Article in journal (Refereed)
    Abstract [en]

    Proteins offer an almost infinite number of functions and geometries for building nanostructures. Here we have focused on amyloid fibrillar proteins as a nanowire template and shown that these fibrils can be coated with the highly conducting polymer alkoxysulfonate PEDOT through molecular self-assembly in water. Transmission electron microscopy and atomic force microscopy show that the coated fibers have a diameter around 15 nm and a length/thickness aspect ratio >1:1000 . We have further shown that networks of the conducting nanowires are electrically and electrochemically active by constructing fully functional electrochemical transistors with nanowire networks, operating at low voltages between 0 and 0.5 V.

  • 8.
    Herland, Anna
    Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics . Linköping University, The Institute of Technology.
    Conjugated Polymers, Amyloid Detection and Assembly of Biomolecular Nanowires2007Doctoral thesis, comprehensive summary (Other academic)
    Abstract [en]

    The research field of conjugated polymers has grown due to the optical and electronic properties of the material, useful in applications such as solar cells and printed electronics, but also in biosensors and for interactions with biomolecules. In this thesis conjugated polymers have been used in two related topics; to detect conformational changes in proteins and to assemble the polymers with biomolecules into nanowires.

    Within biosensing, conjugated polymers have been used for detection of a wide range of biological events, such as DNA hybridization or enzymatic activity, utilizing both electronic and optical changes in the polymer. Here the focus has been to use the polymers as optical probes to discriminate between native and misfolded protein, as well as to follow the misfolding processes in vitro. The understanding and detection of protein misfolding, for example amyloid fibril formation, is a topic of growing importance. The misfolding process is strongly associated with several devastating diseases such as Alzheimer’s disease, Parkinson’s disease and Bovine Spongiform Encephalopathy (BSE). We have developed detection schemes for discrimination between proteins in the native or amyloid fibril state based on luminescent polythiophene derivatives. Through a synthesis strategy based on polymerization of trimer blocks rather than of monomers, polythiophene derivatives with higher optical signal specificity for amyloid-like fibrils were obtained.

    Self-assembly of nanowires containing conjugated polymers is a route to generate structures of unique opto-electrical characteristics without the need for tedious topdown processes. Biomolecules can have nanowire geometries of extraordinary aspect ratio and functionalities. The DNA molecule is the most well known and exploited of these. In this thesis work the more stable amyloid fibril has been used as a template to organize conjugated polymers. Luminescent, semi-conducting, conjugated polymers have been incorporated in and assembled onto amyloid fibrils. Using luminescence quenching we have demonstrated that the conjugated material can retain the electro-activity after the incorporation process. Furthermore, the amyloid fibril/conjugated polymer hybrid structures can be organized on surfaces by the means of molecular combing and soft lithography.

    In the process of generating self-assembled biomolecular nanowires functionalized with conjugated polymers, we have shown a new synthesis strategy for a water-soluble highly conducting polythiophene derivative. This material, PEDOT-S, has shown affinity for amyloid fibrils, but can also be very useful in conventional opto-electronic polymer-based devices.

    List of papers
    1. Synthesis of a regioregular zwitterionic conjugated oligoelectrolyte, usable as an optical probe for detection of amyloid fibril formation at acidic pH
    Open this publication in new window or tab >>Synthesis of a regioregular zwitterionic conjugated oligoelectrolyte, usable as an optical probe for detection of amyloid fibril formation at acidic pH
    Show others...
    2005 (English)In: Journal of the American Chemical Society, ISSN 0002-7863, E-ISSN 1520-5126, Vol. 127, no 7, p. 2317-2323Article in journal (Refereed) Published
    Abstract [en]

    Changes of the optical properties of conjugated polyelectrolytes have been utilized to monitor noncovalent interactions between biomolecules and the conjugated polyelectrolytes in sensor applications. A regioregular, zwitterionic conjugated oligoelectrolyte was synthesized in order to create a probe with a defined set of optical properties and hereby facilitate interpretation of biomolecule−oligoelectrolyte interactions. The synthesized oligoelectrolyte was used at acidic pH as a novel optical probe to detect amyloid fibril formation of bovine insulin and chicken lysozyme. Interaction of the probe with formed amyloid fibrils results in changes of the geometry and the electronic structure of the oligoelectrolyte chains, which were monitored with absorption and emission spectroscopy.

    National Category
    Natural Sciences
    Identifiers
    urn:nbn:se:liu:diva-14598 (URN)10.1021/ja045835e (DOI)
    Available from: 2007-10-12 Created: 2007-10-12 Last updated: 2018-04-25
    2. Conjugated polyelectrolytes: conformation-sensitive optical probes for detection of amyloid fibril formation
    Open this publication in new window or tab >>Conjugated polyelectrolytes: conformation-sensitive optical probes for detection of amyloid fibril formation
    2005 (English)In: Biochemistry, ISSN 0006-2960, E-ISSN 1520-4995, Vol. 44, no 10, p. 3718-3724Article in journal (Refereed) Published
    Abstract [en]

    The in vivo deposition of amyloid fibrils is a hallmark of many devastating diseases known as the amyloidoses. Amyloid formation in vitro may also complicate production of proteins in the biotechnology industry. Simple, sensitive, and versatile tools that detect the fibrillar conformation of amyloidogenic proteins are thus of great importance. We have developed a negatively charged conjugated polyelectrolyte that displays different characteristic optical changes, detected visually or by absorption and emission, depending on whether the protein with which it forms a complex is in its native state or amyloid fibril conformation. This simple, rapid, and novel methodology was applied here to two amyloidogenic proteins, insulin and lysozyme, and its validity for detection of their fibrillar conformation was verified by currently used methods such as circular dichroism, transmission electron microscopy, and Congo red absorption.

    National Category
    Engineering and Technology
    Identifiers
    urn:nbn:se:liu:diva-14599 (URN)10.1021/bi047402u (DOI)
    Available from: 2007-10-12 Created: 2007-10-12 Last updated: 2018-04-25
    3. Studies of luminescent conjugated polythiophene derivatives-Enhanced spectral discrimination of protein conformational states
    Open this publication in new window or tab >>Studies of luminescent conjugated polythiophene derivatives-Enhanced spectral discrimination of protein conformational states
    Show others...
    2007 (English)In: Bioconjugate chemistry, ISSN 1043-1802, E-ISSN 1520-4812, Vol. 18, no 6, p. 1860-1868Article in journal (Refereed) Published
    Abstract [en]

    Improved probes for amyloid fibril formation are advantageous for the early detection and better understanding of this disease-associated process. Here, we report a comparative study of eight luminescent conjugated polythiophene derivates (LCPs) and their discrimination of a protein (insulin) in the native or amyloid-like fibrillar state. For two of the LCPs, the synthesis is reported. Compared to their monomer-based analogues, trimer-based LCPs showed significantly better optical signal specificity for amyloid-like fibrils, seen from increased quantum yield and spectral shift. The trimer-based LCPs alone were highly quenched and showed little interaction with native insulin, as seen from analytical ultracentrifugation and insignificant spectral differences from the trimer-based LCP in buffered and native protein solution. Hence, the trimer-based LCPs showed enhanced discrimination between the amyloid-like fibrillar state and the corresponding native protein.

    National Category
    Natural Sciences
    Identifiers
    urn:nbn:se:liu:diva-14600 (URN)10.1021/bc700180g (DOI)
    Available from: 2007-10-12 Created: 2007-10-12 Last updated: 2018-04-25
    4. Electroactive luminescent self-assembled bio-organic nanowires: Integration of semiconducting oligoelectrolytes within amyloidogenic proteins
    Open this publication in new window or tab >>Electroactive luminescent self-assembled bio-organic nanowires: Integration of semiconducting oligoelectrolytes within amyloidogenic proteins
    Show others...
    2005 (English)In: Advanced Materials, ISSN 0935-9648, Vol. 17, no 12, p. 1466-1471Article in journal (Refereed) Published
    Keywords
    Biomaterials, Luminescence, Nanowires, Peptides, Poly(3, 4-ethylenedioxythiophene) (PEDOT), Self-assembly
    National Category
    Natural Sciences
    Identifiers
    urn:nbn:se:liu:diva-14601 (URN)10.1002/adma.200500183 (DOI)
    Available from: 2007-10-12 Created: 2007-10-12 Last updated: 2018-04-25
    5. Alignment of a conjugated polymer onto amyloid-like protein fibrils
    Open this publication in new window or tab >>Alignment of a conjugated polymer onto amyloid-like protein fibrils
    Show others...
    2007 (English)In: Small, ISSN 1613-6810, Vol. 3, no 2, p. 318-325Article in journal (Refereed) Published
    Abstract [en]

    The amyloid-like fibril is a biomolecular nanowire template of very high stability. Here we describe the coordination of a conjugated polyelectrolyte, poly(thiophene acetic acid) (PTAA), to bovine insulin fibrils with widths of <10 nm and lengths of up to more than 10 m. Fibrils complexed with PTAA are aligned on surfaces through molecular combing and transfer printing. Single-molecule spectroscopy techniques are applied to chart spectral variation in the emission of these wires. When these results are combined with analysis of the polarization of the emitted light, we can conclude that the polymer chains are preferentially aligned along the fibrillar axis.

    Keywords
    fibrils, nanowires, polymers, self-assembly, template synthesis
    National Category
    Physical Sciences
    Identifiers
    urn:nbn:se:liu:diva-14602 (URN)10.1002/smll.200600377 (DOI)
    Available from: 2007-10-12 Created: 2007-10-12 Last updated: 2009-04-29
    6. Decoration of amyloid fibrils with luminescent conjugated polymers
    Open this publication in new window or tab >>Decoration of amyloid fibrils with luminescent conjugated polymers
    Show others...
    2008 (English)In: Journal of Materials Chemistry, ISSN 0959-9428, E-ISSN 1364-5501, Vol. 18, no 1, p. 126-132Article in journal (Refereed) Published
    Abstract [en]

    In this work we report the coating of a biological template with a polar, but uncharged, luminescent conjugated polymer, soluble in organic solvents but not in water, to produce a nanowire. Amyloid fibrils from bovine insulin were decorated with an alternating polyfluorene derivative. Decorated fibrils were partially aligned on hydrophobic surfaces as separate and bundled fibrils, by means of molecular combing. The single molecule spectroscopy technique utilizing excitation by rotating linearly polarized light and fluorescence detection through a rotating polarizer showed a high degree of anisotropy of the polymer chains on the individual fibrils. The high degree of polarization indicated highly oriented polymer chains with the preferential orientation of the polymer backbone along the fibrils. The anisotropy ratios are comparable with those of well-oriented polymer chains in films. © The Royal Society of Chemistry.

    National Category
    Natural Sciences
    Identifiers
    urn:nbn:se:liu:diva-14603 (URN)10.1039/b712829k (DOI)000251580400016 ()
    Available from: 2007-10-12 Created: 2007-10-12 Last updated: 2017-12-13
    7. Iron Catalyzed Polymerization of Alkoxysulfonate-Functionalized EDOT gives
    Open this publication in new window or tab >>Iron Catalyzed Polymerization of Alkoxysulfonate-Functionalized EDOT gives
    Show others...
    2007 (English)In: Chemistry of Materials, ISSN 0897-4756, E-ISSN 1520-5002Article in journal (Refereed) Submitted
    National Category
    Natural Sciences
    Identifiers
    urn:nbn:se:liu:diva-14604 (URN)
    Available from: 2007-10-12 Created: 2007-10-12 Last updated: 2017-12-13
  • 9.
    Herland, Anna
    et al.
    Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics . Linköping University, The Institute of Technology.
    Björk, Per
    Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics . Linköping University, The Institute of Technology.
    Hania, P. Ralph
    Department of Chemical Physics, University of Lund, Lund, Sweden.
    Scheblykin, Ivan G.
    Department of Chemical Physics, University of Lund, Lund, Sweden.
    Inganäs, Olle
    Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics . Linköping University, The Institute of Technology.
    Alignment of a conjugated polymer onto amyloid-like protein fibrils2007In: Small, ISSN 1613-6810, Vol. 3, no 2, p. 318-325Article in journal (Refereed)
    Abstract [en]

    The amyloid-like fibril is a biomolecular nanowire template of very high stability. Here we describe the coordination of a conjugated polyelectrolyte, poly(thiophene acetic acid) (PTAA), to bovine insulin fibrils with widths of <10 nm and lengths of up to more than 10 m. Fibrils complexed with PTAA are aligned on surfaces through molecular combing and transfer printing. Single-molecule spectroscopy techniques are applied to chart spectral variation in the emission of these wires. When these results are combined with analysis of the polarization of the emitted light, we can conclude that the polymer chains are preferentially aligned along the fibrillar axis.

  • 10.
    Herland, Anna
    et al.
    Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics . Linköping University, The Institute of Technology.
    Björk, Per
    Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics . Linköping University, The Institute of Technology.
    Nilsson, K. Peter R.
    Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics . Linköping University, The Institute of Technology.
    Hammarström, Per
    Linköping University, Department of Physics, Chemistry and Biology, Biochemistry. Linköping University, The Institute of Technology.
    Inganäs, Olle
    Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics . Linköping University, The Institute of Technology.
    Konradsson, Peter
    Linköping University, Department of Physics, Chemistry and Biology, Organic Chemistry . Linköping University, The Institute of Technology.
    Electroactive luminescent self-assembled bio-organic nanowires: Integration of semiconducting oligoelectrolytes within amyloidogenic proteins2005In: Advanced Materials, ISSN 0935-9648, Vol. 17, no 12, p. 1466-1471Article in journal (Refereed)
  • 11.
    Herland, Anna
    et al.
    Linköping University, The Institute of Technology. Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics .
    Inganäs, Olle
    Linköping University, The Institute of Technology. Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics .
    Conjugated polymers as optical probes for protein interactions and protein conformations2007In: Macromolecular rapid communications, ISSN 1022-1336, E-ISSN 1521-3927, Vol. 28, no 17, p. 1703-1713Article in journal (Refereed)
    Abstract [en]

    There is a need for highly sensitive, multi-parallel protein sensors within diagnostics and proteomic research. Conjugated polymers (CPs) have been demonstrated as highly sensitive optical probes for protein biosensing. Compared to small molecules, the polymeric probe has the possibility of multiple interactions and a collective response, which enhances the sensor signal. The optical output is colorimetric or, more sensitive, fluorescence based, including Förster energy transfer and changes in the emission wavelengths and/or intensity. Using CPs, many interesting protein detection events have been demonstrated, e.g., protein interactions, enzymatic activity, amyloid fibril formation, and detection by aptamers. CPs have also been successfully used to stain bacterial, cellular, and tissue samples. © 2007 WILEY-VCH Verlag GmbH & Co. KGaA.

  • 12.
    Herland, Anna
    et al.
    Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics . Linköping University, The Institute of Technology.
    Nilsson, K. Peter R.
    Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics . Linköping University, The Institute of Technology.
    Olsson, Johan D. M.
    Linköping University, Department of Physics, Chemistry and Biology. Linköping University, The Institute of Technology.
    Hammarström, Per
    Linköping University, Department of Physics, Chemistry and Biology, Biochemistry. Linköping University, The Institute of Technology.
    Konradsson, Peter
    Linköping University, Department of Physics, Chemistry and Biology, Organic Chemistry . Linköping University, The Institute of Technology.
    Inganäs, Olle
    Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics . Linköping University, The Institute of Technology.
    Synthesis of a regioregular zwitterionic conjugated oligoelectrolyte, usable as an optical probe for detection of amyloid fibril formation at acidic pH2005In: Journal of the American Chemical Society, ISSN 0002-7863, E-ISSN 1520-5126, Vol. 127, no 7, p. 2317-2323Article in journal (Refereed)
    Abstract [en]

    Changes of the optical properties of conjugated polyelectrolytes have been utilized to monitor noncovalent interactions between biomolecules and the conjugated polyelectrolytes in sensor applications. A regioregular, zwitterionic conjugated oligoelectrolyte was synthesized in order to create a probe with a defined set of optical properties and hereby facilitate interpretation of biomolecule−oligoelectrolyte interactions. The synthesized oligoelectrolyte was used at acidic pH as a novel optical probe to detect amyloid fibril formation of bovine insulin and chicken lysozyme. Interaction of the probe with formed amyloid fibrils results in changes of the geometry and the electronic structure of the oligoelectrolyte chains, which were monitored with absorption and emission spectroscopy.

  • 13.
    Herland, Anna
    et al.
    Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics . Linköping University, The Institute of Technology.
    Thomsson, Daniel
    University of Lund.
    Mirzov, Oleg
    University of Lund.
    Scheblykin, Ivan G.
    University of Lund.
    Inganäs, Olle
    Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics . Linköping University, The Institute of Technology.
    Decoration of amyloid fibrils with luminescent conjugated polymers2008In: Journal of Materials Chemistry, ISSN 0959-9428, E-ISSN 1364-5501, Vol. 18, no 1, p. 126-132Article in journal (Refereed)
    Abstract [en]

    In this work we report the coating of a biological template with a polar, but uncharged, luminescent conjugated polymer, soluble in organic solvents but not in water, to produce a nanowire. Amyloid fibrils from bovine insulin were decorated with an alternating polyfluorene derivative. Decorated fibrils were partially aligned on hydrophobic surfaces as separate and bundled fibrils, by means of molecular combing. The single molecule spectroscopy technique utilizing excitation by rotating linearly polarized light and fluorescence detection through a rotating polarizer showed a high degree of anisotropy of the polymer chains on the individual fibrils. The high degree of polarization indicated highly oriented polymer chains with the preferential orientation of the polymer backbone along the fibrils. The anisotropy ratios are comparable with those of well-oriented polymer chains in films. © The Royal Society of Chemistry.

  • 14.
    Karlsson, Roger H.
    et al.
    Linköping University, Department of Physics, Chemistry and Biology. Linköping University, The Institute of Technology.
    Herland, Anna
    Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics . Linköping University, The Institute of Technology.
    Hamedi, Mahiar
    Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics . Linköping University, The Institute of Technology.
    Åslund, Andreas
    Linköping University, Department of Physics, Chemistry and Biology, Organic Chemistry . Linköping University, The Institute of Technology.
    Inganäs, Olle
    Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics . Linköping University, The Institute of Technology.
    Konradsson, Peter
    Linköping University, Department of Physics, Chemistry and Biology, Organic Chemistry . Linköping University, The Institute of Technology.
    Iron Catalyzed Polymerization of Alkoxysulfonate-Functionalized EDOT gives2007In: Chemistry of Materials, ISSN 0897-4756, E-ISSN 1520-5002Article in journal (Refereed)
  • 15.
    Karlsson, Roger
    et al.
    Linköping University, Department of Physics, Chemistry and Biology, Organic Chemistry. Linköping University, The Institute of Technology.
    Herland, Anna
    Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics. Linköping University, The Institute of Technology.
    Hamedi, Mahiar
    Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics. Linköping University, The Institute of Technology.
    Wigenius, Jens
    Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics. Linköping University, The Institute of Technology.
    Åslund, Andreas
    Linköping University, Department of Physics, Chemistry and Biology, Organic Chemistry. Linköping University, The Institute of Technology.
    Liu, Xianjie
    Linköping University, Department of Physics, Chemistry and Biology, Surface Physics and Chemistry. Linköping University, The Institute of Technology.
    Fahlman, Mats
    Linköping University, Department of Physics, Chemistry and Biology, Surface Physics and Chemistry. Linköping University, The Institute of Technology.
    Inganäs, Olle
    Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics. Linköping University, The Institute of Technology.
    Konradsson, Peter
    Linköping University, Department of Physics, Chemistry and Biology, Organic Chemistry. Linköping University, The Institute of Technology.
    Iron-Catalyzed Polymerization of Alkoxysulfonate-Functionalized 3,4-Ethylenedioxythiophene Gives Water-Soluble Poly(3,4-ethylenedioxythiophene) of High Conductivity2009In: Chemistry of Materials, ISSN 0897-4756, E-ISSN 1520-5002, Vol. 21, no 9, p. 1815-1821Article in journal (Refereed)
    Abstract [en]

    Chemical polymerization of a 3,4-ethylenedioxythiophene derivative bearing a sulfonate group (EDOTS) is reported. The polymer, PEDOT-S, is fully water-soluble and has been produced by polymerizing EDOT-S in water, using Na2S2O8 and a catalytic amount of FeCl3. Elemental analysis and XPS measurements indicate that PEDOT-S is a material with a substantial degree of self-doping, but also contains free sulfate ions as charge-balancing counterions of the oxidized polymer. Apart from self-doping PEDOT-S, the side chains enable full water solubility of the material; DLS studies show an average cluster size of only 2 nm. Importantly, the solvation properties of the PEDOT-S are reflected in spin-coated films, which show a surface roughness of 1.2 nm and good conductivity (12 S/cm) in ambient conditions. The electro-optical properties of this material are shown with cyclic voltammetry and spectroelectrochemical experiment reveals an electrochromic contrast (similar to 48% at lambda(max) = 606 nm).

  • 16.
    Nilsson, Peter
    et al.
    Linköping University, The Institute of Technology. Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics .
    Hammarström, Per
    Linköping University, The Institute of Technology. Linköping University, Department of Physics, Chemistry and Biology, Biochemistry.
    Ahlgren, Fredrik
    Division of Cell Biology Linköpings universitet.
    Herland, Anna
    Linköping University, The Institute of Technology. Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics .
    Schnell, Edrun A
    The Norwegian University of Science and Technology.
    Lindgren, Mikael
    The Norwegian University of Science and Technology.
    Westermark, Gunilla
    Linköping University, Faculty of Health Sciences. Linköping University, Department of Biomedicine and Surgery, Division of cell biology.
    Inganäs, Olle
    Linköping University, The Institute of Technology. Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics .
    Conjugated Polyelectrolytes - Conformation - Sensitive Optical Probes for staining and Characterization of Amyloid Deposits2006In: ChemBioChem (Print), ISSN 1439-4227, E-ISSN 1439-7633, Vol. 7, p. 1096-1104Article in journal (Refereed)
    Abstract [en]

      

  • 17.
    Nilsson, Peter
    et al.
    Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics. Linköping University, The Institute of Technology.
    Herland, Anna
    Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics. Linköping University, The Institute of Technology.
    Hammarström, Per
    Linköping University, Department of Physics, Chemistry and Biology, Biochemistry. Linköping University, The Institute of Technology.
    Inganäs, Olle
    Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics. Linköping University, The Institute of Technology.
    Conjugated polyelectrolytes: conformation-sensitive optical probes for detection of amyloid fibril formation2005In: Biochemistry, ISSN 0006-2960, E-ISSN 1520-4995, Vol. 44, no 10, p. 3718-3724Article in journal (Refereed)
    Abstract [en]

    The in vivo deposition of amyloid fibrils is a hallmark of many devastating diseases known as the amyloidoses. Amyloid formation in vitro may also complicate production of proteins in the biotechnology industry. Simple, sensitive, and versatile tools that detect the fibrillar conformation of amyloidogenic proteins are thus of great importance. We have developed a negatively charged conjugated polyelectrolyte that displays different characteristic optical changes, detected visually or by absorption and emission, depending on whether the protein with which it forms a complex is in its native state or amyloid fibril conformation. This simple, rapid, and novel methodology was applied here to two amyloidogenic proteins, insulin and lysozyme, and its validity for detection of their fibrillar conformation was verified by currently used methods such as circular dichroism, transmission electron microscopy, and Congo red absorption.

  • 18.
    Nilsson, Peter
    et al.
    Linköping University, Department of Physics, Chemistry and Biology, Organic Chemistry. Linköping University, The Institute of Technology.
    Åslund, Andreas
    Linköping University, The Institute of Technology. Linköping University, Department of Physics, Chemistry and Biology, Organic Chemistry.
    Berg, Ina
    Nyström, Sofie
    Linköping University, The Institute of Technology. Linköping University, Department of Physics, Chemistry and Biology, Biochemistry.
    Konradsson, Peter
    Linköping University, The Institute of Technology. Linköping University, Department of Physics, Chemistry and Biology, Organic Chemistry.
    Herland, Anna
    Linköping University, The Institute of Technology. Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics.
    Inganäs, Olle
    Linköping University, The Institute of Technology. Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics.
    Stabo-Eeg, Frantz
    Lindgren, Mikael
    Westermark, Gunilla
    Linköping University, Faculty of Health Sciences. Linköping University, Department of Biomedicine and Surgery, Division of cell biology.
    Lannfelt, Lars
    Nilsson, Lars N G
    Hammarström, Per
    Linköping University, The Institute of Technology. Linköping University, Department of Physics, Chemistry and Biology, Biochemistry.
    Imaging distinct conformational states of amyloid-β fibrils in Alzheimer's disease using novel luminescent probes2007In: ACS Chemical Biology, ISSN 1554-8929, Vol. 2, no 8, p. 553-560Article in journal (Refereed)
    Abstract [en]

    Using luminescent conjugated polyelectrolyte probes (LCPs), we demonstrate the possibility to distinguish amyloid-β 1-42 peptide (Aβ1-42) fibril conformations, by analyzing in vitro generated amyloid fibrils of Aβ1-42 formed under quiescent and agitated conditions. LCPs were then shown to resolve such conformational heterogeneity of amyloid deposits in vivo. A diversity of amyloid deposits depending upon morphology and anatomic location was illustrated with LCPs in frozen ex vivo brain sections from a transgenic mouse model (tg-APPswe) of Alzheimer's disease. Comparative LCP fluorescence showed that compact-core plaques of amyloid β precursor protein transgenic mice were composed of rigid dense amyloid. A more abundant form of amyloid plaque displayed morphology of a compact center with a protruding diffuse exterior. Surprisingly, the compact center of these plaques showed disordered conformations of the fibrils, and the exterior was composed of rigid amyloid protruding from the disordered center. This type of plaque appears to grow from more loosely assembled regions toward solidified amyloid tentacles. This work demonstrates how application of LCPs can prove helpful to monitor aggregate structure of in vivo formed amyloid deposits such as architecture, maturity, and origin.

  • 19.
    Petoral Jr., Rodrigo M.
    et al.
    Linköping University, Department of Physics, Chemistry and Biology, Applied Physics. Linköping University, The Institute of Technology.
    Herland, Anna
    Linköping University, Department of Physics, Chemistry and Biology, Applied Physics. Linköping University, The Institute of Technology.
    Broo, Kerstin
    Linköping University, Department of Physics, Chemistry and Biology, Applied Physics. Linköping University, The Institute of Technology.
    Uvdal, Kajsa
    Linköping University, Department of Physics, Chemistry and Biology, Applied Physics. Linköping University, The Institute of Technology.
    G-protein interactions with receptor-derived peptides chemisorbed on gold2003In: Langmuir, ISSN 0743-7463, E-ISSN 1520-5827, Vol. 19, no 24, p. 10304-10309Article in journal (Refereed)
    Abstract [en]

    Interactions between the functional bovine brain G-protein and receptor-derived peptidea chemically adsorbed on gold surfaces are studied. The peptides are designed to mimic the third ic-loop (aa 361-373) of the Alpha 2a-adrenergic receptor (α 2AR). These segments are linked to a surface using the thiol-gold chemistry, and the protein interaction studies are conducted to investigate the key function of recognition. The chemical composition and binding strength of the peptide monolayers onto a gold surface are characterized using X-ray photoelectron spectroscopy and infrared (IR) spectroscopy. Strong molecular binding of the adsorbates to the gold surface is attained, and the presence of amide-related IR vibrations verified the composition of the peptides. Bovine brain G-protein adsorption studies on these molecular monolayers are performed using the surface plasmon resonance technique. The arginine-rich peptide, which is a direct mimicry of the receptor, has a higher affinity for G-protein than the lysine-rich and alanine-rich derived peptides, showing that arginine residue has special importance for the G-protein interaction with the receptor.

  • 20.
    Tanaka, H.
    et al.
    Kyushu University.
    Herland, Anna
    Linköping University, The Institute of Technology. Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics .
    Lindgren, L.J.
    Chalmers univeristy of Technology.
    Tsutsui, T.
    Kyushu University.
    Andersson, Mats R
    Chalmers univeristy of Technology.
    Inganäs, Olle
    Linköping University, The Institute of Technology. Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics .
    Enhanced current efficiency from Bio-Organic light-emitting diodes using decorated amyloid fibrils with conjugated polymer2008In: Nano letters (Print), ISSN 1530-6984, E-ISSN 1530-6992, Vol. 8, no 9, p. 2858-2861Article in journal (Refereed)
    Abstract [en]

    We demonstrate the use of self-assembled bionanostructures in polymer light-emitting diodes. Amyloid fibrils formed by protein misfolding were decorated with a soluble luminescent conjugated polymer. This conjugated polymer complex with amyloid fibrils was used as the active layer in a light emitting diode, resulting in a 10-fold increase in external quantum efficiency compared with pristine polymer, because of improved carrier injection. © 2008 American Chemical Society.

  • 21. Wirehn, J.
    et al.
    Carlsson, Karin
    Linköping University, The Institute of Technology. Linköping University, Department of Physics, Chemistry and Biology, Biochemistry.
    Herland, Anna
    Linköping University, The Institute of Technology. Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics .
    Persson, E.
    Haemostasis Biochemistry, Novo Nordisk A/S, Novo Nordisk Park, 2760 Måløv, Denmark.
    Carlsson, Uno
    Linköping University, The Institute of Technology. Linköping University, Department of Physics, Chemistry and Biology, Biochemistry.
    Svensson, Magdalena
    Linköping University, The Institute of Technology. Linköping University, Department of Physics, Chemistry and Biology, Biochemistry.
    Hammarström, Per
    Linköping University, The Institute of Technology. Linköping University, Department of Physics, Chemistry and Biology, Biochemistry.
    Activity, folding, misfolding, and aggregation in vitro of the naturally occurring human tissue factor mutant R200W2005In: Biochemistry, ISSN 0006-2960, E-ISSN 1520-4995, Vol. 44, no 18, p. 6755-6763Article in journal (Refereed)
    Abstract [en]

    Tissue factor (TF), a small transmembrane receptor, binds factor VIIa (FVIIa), and the formed complex initiates blood coagulation by proteolytic activation of substrate factors IX and X. A naturally occurring mutation in the human TF gene was recently reported, where a single-base substitution results in an R200W mutation in the TF extracellular domain [Zawadzki, C., Preudhomme, C., Gavériaux, V., Amouyel, P., and Jude, B. (2002) Thromb. Haemost. 87, 540-541]. This mutation appears to be associated with low monocyte TF expression and may protect against thrombosis but has not been associated with any pathological condition, and individuals who present the heterozygous trait appear healthy. Here, we report the activity, folding, and aggregation behavior of the R200W mutant of the 219-residue soluble extracellular domain of TF (sTFR200W) compared to that of the wild-type protein (sTF wt). No differences in stability or FVIIa cofactor activity but an impaired ability to promote FX activation at physiological conditions between the sTFR200W mutant and sTFwt were evident. Increased binding of 1-anilino-8-naphthalene-sulfonic acid (ANS) to sTFR200W indicated a population of partially folded intermediates during denaturation. sTFR200W showed a dramatically increased propensity for aggregate formation compared to sTFwt at mildly acidic pHs, with an increased rate of aggregation during conditions, promoting the intermediate state. The lowered pH resistance could explain the loss of sTFR200W in vivo because of aggregation of the mutant. The intrinsic structure of the sTF aggregates appears reminiscent of amyloid fibrils, as revealed by thioflavin T fluorescence, atomic force microscopy, and transmission electron microscopy. We conclude that the lowered activity for FX activation and the propensity of the mutant protein to misfold and aggregate will both contribute to decreased coagulation activity in TFR200W carriers, which could protect from thrombotic disease. © 2005 American Chemical Society.

  • 22.
    Åslund, Andreas
    et al.
    Linköping University, Department of Physics, Chemistry and Biology, Organic Chemistry. Linköping University, The Institute of Technology.
    Herland, Anna
    Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics. Linköping University, The Institute of Technology.
    Hammarström, Per
    Linköping University, Department of Physics, Chemistry and Biology, Biochemistry. Linköping University, The Institute of Technology.
    Nilsson, Peter
    Linköping University, Department of Physics, Chemistry and Biology, Organic Chemistry. Linköping University, The Institute of Technology.
    Jonsson, Bengt-Harald
    Linköping University, Department of Physics, Chemistry and Biology, Molecular Biotechnology. Linköping University, The Institute of Technology.
    Inganäs, Olle
    Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics. Linköping University, The Institute of Technology.
    Konradsson, Peter
    Linköping University, Department of Physics, Chemistry and Biology, Organic Chemistry. Linköping University, The Institute of Technology.
    Studies of luminescent conjugated polythiophene derivatives-Enhanced spectral discrimination of protein conformational states2007In: Bioconjugate chemistry, ISSN 1043-1802, E-ISSN 1520-4812, Vol. 18, no 6, p. 1860-1868Article in journal (Refereed)
    Abstract [en]

    Improved probes for amyloid fibril formation are advantageous for the early detection and better understanding of this disease-associated process. Here, we report a comparative study of eight luminescent conjugated polythiophene derivates (LCPs) and their discrimination of a protein (insulin) in the native or amyloid-like fibrillar state. For two of the LCPs, the synthesis is reported. Compared to their monomer-based analogues, trimer-based LCPs showed significantly better optical signal specificity for amyloid-like fibrils, seen from increased quantum yield and spectral shift. The trimer-based LCPs alone were highly quenched and showed little interaction with native insulin, as seen from analytical ultracentrifugation and insignificant spectral differences from the trimer-based LCP in buffered and native protein solution. Hence, the trimer-based LCPs showed enhanced discrimination between the amyloid-like fibrillar state and the corresponding native protein.

1 - 22 of 22
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