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  • 1.
    Boesze-Battaglia, Kathleen
    et al.
    University of Penn, PA 19104 USA.
    Walker, Lisa P.
    University of Penn, PA 19104 USA.
    Zekavat, Ali
    University of Penn, PA 19104 USA.
    Dlakic, Mensur
    Montana State University, MT 59717 USA.
    Damek Scuron, Monika
    University of Penn, PA 19104 USA.
    Nygren, Patrik
    Linköpings universitet, Institutionen för fysik, kemi och biologi, Kemi. Linköpings universitet, Tekniska fakulteten.
    Shenker, Bruce J.
    University of Penn, PA 19104 USA.
    The Aggregatibacter actinomycetemcomitans Cytolethal Distending Toxin Active Subunit CdtB Contains a Cholesterol Recognition Sequence Required for Toxin Binding and Subunit Internalization2015Inngår i: Infection and Immunity, ISSN 0019-9567, E-ISSN 1098-5522, Vol. 83, nr 10, s. 4042-4055Artikkel i tidsskrift (Fagfellevurdert)
    Abstract [en]

    Induction of cell cycle arrest in lymphocytes following exposure to the Aggregatibacter actinomycetemcomitans cytolethal distending toxin (Cdt) is dependent upon the integrity of lipid membrane microdomains. Moreover, we have previously demonstrated that the association of Cdt with target cells involves the CdtC subunit which binds to cholesterol via a cholesterol recognition amino acid consensus sequence (CRAC site). In this study, we demonstrate that the active Cdt subunit, CdtB, also is capable of binding to large unilamellar vesicles (LUVs) containing cholesterol. Furthermore, CdtB binding to cholesterol involves a similar CRAC site as that demonstrated for CdtC. Mutation of the CRAC site reduces binding to model membranes as well as toxin binding and CdtB internalization in both Jurkat cells and human macrophages. A concomitant reduction in Cdt-induced toxicity was also noted, indicated by reduced cell cycle arrest and apoptosis in Jurkat cells and a reduction in the proinflammatory response in macrophages (interleukin 1 beta [IL-1 beta] and tumor necrosis factor alpha [TNF-alpha] release). Collectively, these observations indicate that membrane cholesterol serves as an essential ligand for both CdtC and CdtB and, further, that this binding is necessary for both internalization of CdtB and subsequent molecular events leading to intoxication of cells.

  • 2.
    Ederth, Thomas
    et al.
    Linköpings universitet, Institutionen för fysik, kemi och biologi, Sensorvetenskap och Molekylfysik. Linköpings universitet, Tekniska högskolan.
    Nygren, Patrik
    Linköpings universitet, Institutionen för fysik, kemi och biologi, Sensorvetenskap och Molekylfysik. Linköpings universitet, Tekniska högskolan.
    Ekblad, Tobias
    Linköpings universitet, Institutionen för fysik, kemi och biologi, Sensorvetenskap och Molekylfysik. Linköpings universitet, Tekniska högskolan.
    Östblom, Mattias
    Linköpings universitet, Institutionen för fysik, kemi och biologi, Sensorvetenskap och Molekylfysik. Linköpings universitet, Tekniska högskolan.
    Liedberg, Bo
    Linköpings universitet, Institutionen för fysik, kemi och biologi, Sensorvetenskap och Molekylfysik. Linköpings universitet, Tekniska högskolan.
    Pettitt, M.E.
    The University of Birmingham, School of Biosciences, Birmingham, UK.
    Callow, M.E.
    The University of Birmingham, School of Biosciences, Birmingham, UK.
    Callow, J.A.
    The University of Birmingham, School of Biosciences, Birmingham, UK.
    Interactions of algal spores and diatoms with mixed synthetic peptide SAMs2007Konferansepaper (Annet vitenskapelig)
  • 3.
    Ederth, Thomas
    et al.
    Linköpings universitet, Institutionen för fysik, kemi och biologi, Sensorvetenskap och Molekylfysik. Linköpings universitet, Tekniska högskolan.
    Nygren, Patrik
    Linköpings universitet, Institutionen för fysik, kemi och biologi, Sensorvetenskap och Molekylfysik. Linköpings universitet, Tekniska högskolan.
    Pettitt, M. E.
    University of Birmingham.
    Oumlstblom, M.
    Linköpings universitet, Institutionen för fysik, kemi och biologi. Linköpings universitet, Tekniska högskolan.
    Du, Chun-Xia
    Linköpings universitet, Institutionen för fysik, kemi och biologi. Linköpings universitet, Tekniska högskolan.
    Broo, Klas
    Linköpings universitet, Institutionen för fysik, kemi och biologi. Linköpings universitet, Tekniska högskolan.
    Callow, M. E.
    University of Birmingham.
    Callow, J.
    University of Birmingham.
    Liedberg, Bo
    Linköpings universitet, Institutionen för fysik, kemi och biologi, Sensorvetenskap och Molekylfysik. Linköpings universitet, Tekniska högskolan.
    Anomalous settlement behavior of Ulva linza zoospores on cationic oligopeptide surfaces2008Inngår i: Biofouling (Print), ISSN 0892-7014, E-ISSN 1029-2454, Vol. 24, nr 4, s. 303-312Artikkel i tidsskrift (Fagfellevurdert)
    Abstract [en]

    Identification of settlement cues for marine fouling organisms opens up new strategies and methods for biofouling prevention, and enables the development of more effective antifouling materials. To this end, the settlement behaviour of zoospores of the green alga Ulva linza onto cationic oligopeptide self-assembled monolayers (SAMs) has been investigated. The spores interact strongly with lysine- and arginine-rich SAMs, and their settlement appears to be stimulated by these surfaces. Of particular interest is an arginine-rich oligopeptide, which is effective in attracting spores to the surface, but in a way which leaves a large fraction of the settled spores attached to the surface in an anomalous fashion. These 'pseudo-settled' spores are relatively easily detached from the surface and do not undergo the full range of cellular responses associated with normal commitment to settlement. This is a hitherto undocumented mode of settlement, and surface dilution of the arginine-rich peptide with a neutral triglycine peptide demonstrates that both normal and anomalous settlement is proportional to the surface density of the arginine-rich peptide. The settlement experiments are complemented with physical studies of the oligopeptide SAMs, before and after extended immersion in artificial seawater, using infrared spectroscopy, null ellipsometry and contact angle measurements.

  • 4.
    Ederth, Thomas
    et al.
    Linköpings universitet, Institutionen för fysik, kemi och biologi, Sensorvetenskap och Molekylfysik. Linköpings universitet, Tekniska högskolan.
    Pettitt, M E
    University of Birmingham.
    Nygren, Patrik
    Linköpings universitet, Institutionen för fysik, kemi och biologi, Sensorvetenskap och Molekylfysik. Linköpings universitet, Tekniska högskolan.
    Du, Chun-Xia
    Linköpings universitet, Institutionen för fysik, kemi och biologi, Molekylär fysik. Linköpings universitet, Tekniska fakulteten.
    Ekblad, Tobias
    Linköpings universitet, Institutionen för fysik, kemi och biologi, Sensorvetenskap och Molekylfysik. Linköpings universitet, Tekniska högskolan.
    Zhou, Ye
    Linköpings universitet, Institutionen för fysik, kemi och biologi, Sensorvetenskap och Molekylfysik. Linköpings universitet, Tekniska högskolan.
    Falk, Magnus
    Linköpings universitet, Institutionen för fysik, kemi och biologi, Molekylär fysik. Linköpings universitet, Tekniska fakulteten.
    Callow, M E
    University of Birmingham.
    Callow, J A
    University of Birmingham.
    Liedberg, Bo
    Linköpings universitet, Institutionen för fysik, kemi och biologi, Sensorvetenskap och Molekylfysik. Linköpings universitet, Tekniska högskolan.
    Interactions of Zoospores of Ulva linza with Arginine-Rich Oligopeptide Monolayers2009Inngår i: Langmuir, ISSN 0743-7463, E-ISSN 1520-5827, Vol. 25, nr 16, s. 9375-9383Artikkel i tidsskrift (Fagfellevurdert)
    Abstract [en]

    We recently reported oil the strong interactions of zoospores of the green alga, Ulva linza with all arginine-rich oligopeptide self-assembled monolayer (SAM) [Biofouling 2008, 24, 303-312], where the arginine-rich peptide induced not only high spore settlement, but also a form of abnormal settlement, or "pseudo-settlement", whereby it proportion of spores do not go through the normal process of surface exploration, adhesive exocytosis, and loss of flagella. Further. it was demonstrated that both the total number of settled spores and the fraction of pseudosettled spores were related to the surface density of the arginine-rich peptide. Here we present a further investigation of the interactions of zoospores of ulva with a set of oligomeric, de nom designed, arginine-rich peptides, specifically aimed to test the effect of peptide primary structure on the interaction. Via variations in the peptide length and by permutations in the amino acid sequences, we gain further insight into the spore-surface interactions. The interpretation of the biological assays is supported by physicochemical characterization of the SAMs using infrared spectroscopy, ellipsometry, and contact angle measurement. Results confirm the importance of arginine residues for the anomalous pseudosettlement, and we found that settlement is modulated by variations in both the total length and peptide primary structure. To elucidate the Causes of the anomalous settlement and the possible relation to peptide-membrane interactions, we also compared the settlement of the "naked" zoospores of Ulva(which present it lipoprotein membrane to the exterior without a discrete polysaccharide cell wall), with the settlement of diatoms (unicellular algae that are surrounded by it silica cell wall), onto the peptide SAMs. Cationic SAMs do not notably affect settlement (attachment), adhesion strength, or viability of diatom cells, Suggesting that the effect of the peptides on zoospores of Ulva is mediated via specific peptide-membrane interactions.

  • 5.
    Johansson, Leif B. G.
    et al.
    Linköpings universitet, Institutionen för fysik, kemi och biologi, Kemi. Linköpings universitet, Tekniska fakulteten.
    Bäck, Marcus
    Linköpings universitet, Institutionen för fysik, kemi och biologi, Kemi. Linköpings universitet, Tekniska fakulteten.
    Lantz, Linda
    Linköpings universitet, Institutionen för fysik, kemi och biologi, Kemi. Linköpings universitet, Tekniska fakulteten.
    Eriksson, Mikaela
    Linköpings universitet, Institutionen för fysik, kemi och biologi, Kemi. Linköpings universitet, Tekniska fakulteten.
    Nygren, Patrik
    Linköpings universitet, Institutionen för fysik, kemi och biologi, Kemi. Linköpings universitet, Tekniska fakulteten.
    Nilsson, Peter R.
    Linköpings universitet, Institutionen för fysik, kemi och biologi, Kemi. Linköpings universitet, Tekniska fakulteten.
    A variety of thiophene based ligands for detection of protein aggregates by surface plasmon resonanceManuskript (preprint) (Annet vitenskapelig)
    Abstract [en]

    By attaching an azide functional group via a tetraethylene glycol linker to the α-terminal position of a variety of oligothiophenes, thiophene-based ligands that can be utilized for detection of protein aggregates with surface plasmon resonance have been developed. All ligands displayed selectivity towards recombinant amyloid fibrils and the LCO/protein aggregate interaction could be detected by fluorescence as well as by surface plasmon resonance.

  • 6.
    Jonsson, Bengt-Harald
    et al.
    Linköpings universitet, Tekniska högskolan. Linköpings universitet, Institutionen för fysik, kemi och biologi, Molekylär Bioteknik.
    Broo, Klas
    Lundqvist, Martin
    Linköpings universitet, Tekniska högskolan. Linköpings universitet, Institutionen för fysik, kemi och biologi, Molekylär Bioteknik.
    Nygren, Patrik
    Linköpings universitet, Tekniska högskolan. Linköpings universitet, Institutionen för fysik, kemi och biologi, Sensorvetenskap och Molekylfysik.
    Design of Functional Peptide-Nanoparticle Complexes with Potential Applications in Targeted Drug Delivery2008Inngår i: BITs 6th annual congress of 2008 International drug discovery science and technology,2008, 2008, s. 142-143Konferansepaper (Annet vitenskapelig)
  • 7.
    Lundqvist, Martin
    et al.
    Linköpings universitet, Institutionen för fysik, kemi och biologi, Molekylär Bioteknik. Linköpings universitet, Tekniska högskolan.
    Nygren, Patrik
    Linköpings universitet, Institutionen för fysik, kemi och biologi, Molekylär Bioteknik. Linköpings universitet, Tekniska högskolan.
    Jonsson, Bengt-Harald
    Linköpings universitet, Institutionen för fysik, kemi och biologi, Molekylär Bioteknik. Linköpings universitet, Tekniska högskolan.
    Broo, Klas
    Linköpings universitet, Institutionen för fysik, kemi och biologi, Tillämpad optik. Linköpings universitet, Tekniska högskolan.
    Induction of structure and function in a designed peptide upon adsorption on a silica nanoparticle2006Inngår i: Angewandte Chemie International Edition, ISSN 1433-7851, E-ISSN 1521-3773, Vol. 45, nr 48, s. 8169-8173Artikkel i tidsskrift (Fagfellevurdert)
    Abstract [en]

    No abstrack available.

  • 8.
    Nygren, Patrik
    Linköpings universitet, Institutionen för fysik, kemi och biologi, Sensorvetenskap och Molekylfysik. Linköpings universitet, Tekniska högskolan.
    De Novo Design and Characterization of Surface Binding Peptides - Steps toward Functional Surfaces2006Licentiatavhandling, med artikler (Annet vitenskapelig)
    Abstract [en]

    The ability to create surfaces with well-defined chemical properties is a major research field. One possibility to do this is to design peptides that bind with a specific secondary structure to silica nanoparticles. The peptides discussed in this thesis are constructed to be random coil in solution, but are “forced” to become helical when adsorbed to the particles. The positively charged side-chains on the peptides strongly disfavor an ordered structure in solution due to electrostatic repulsion. When the peptides are introduced to the particles these charges will strongly favor the structure because of ion pair bonding between the peptide and the negatively charged nanoparticles. The peptide-nanoparticle system has been thoroughly investigated by systematic variations of the side-chains. In order to determine which factors that contributes to the induced structure, several peptides with different amino acid sequences have been synthesized. Factors that have been investigated include 1) the positive charge density, 2) distribution of positive charges, 3) negative charge density, 4) increasing hydrophobicity, 5) peptide length, and 6) by incorporating amino acids with different helix propensities. Moreover, pH dependence and the effect of different nanoparticle curvature have also been investigated. It will also be shown that the system can be modified to incorporate a catalytic site that is only active when the helix is formed. This research will increase our understanding of peptide-surface interactions and might be of importance for both nanotechnology and medicine.

    Delarbeid
    1. Induction of structure and function in a designed peptide upon adsorption on a silica nanoparticle
    Åpne denne publikasjonen i ny fane eller vindu >>Induction of structure and function in a designed peptide upon adsorption on a silica nanoparticle
    2006 (engelsk)Inngår i: Angewandte Chemie International Edition, ISSN 1433-7851, E-ISSN 1521-3773, Vol. 45, nr 48, s. 8169-8173Artikkel i tidsskrift (Fagfellevurdert) Published
    Abstract [en]

    No abstrack available.

    Emneord
    Amino acids, catalysis, helical structures, nanoparticles, peptides
    HSV kategori
    Identifikatorer
    urn:nbn:se:liu:diva-14548 (URN)10.1002/anie.200600965 (DOI)
    Tilgjengelig fra: 2008-02-25 Laget: 2008-02-25 Sist oppdatert: 2017-12-13bibliografisk kontrollert
    2. Optimizing Nanoparticle Induced Helical Structure in a De Novo Designed Peptide by Rational Changes in Amino Acid Sequence
    Åpne denne publikasjonen i ny fane eller vindu >>Optimizing Nanoparticle Induced Helical Structure in a De Novo Designed Peptide by Rational Changes in Amino Acid Sequence
    Manuskript (Annet vitenskapelig)
    Identifikatorer
    urn:nbn:se:liu:diva-14549 (URN)
    Tilgjengelig fra: 2008-02-25 Laget: 2008-02-25 Sist oppdatert: 2010-01-13
  • 9.
    Nygren, Patrik
    Linköpings universitet, Institutionen för fysik, kemi och biologi, Sensorvetenskap och Molekylfysik. Linköpings universitet, Tekniska högskolan.
    Structural and Functional Studies of De Novo Designed Peptides at Surfaces2008Doktoravhandling, med artikler (Annet vitenskapelig)
    Abstract [en]

    The work presented in this thesis deals with the structural and functional properties of peptides at surfaces. The interaction of peptides with surfaces is an ever so common occurrence in our every day life, from the bug squashed on the windshield of our car to the barnacle on our boat, and from the blood plasma used in the hospital to the proteins in our cells. The effect these occurrences has on our lives is diverse, the bug is annoying whereas the barnacle settlement of ship hull is costly for marine transportation, the blood plasma contains components of vital importance for our immunological defense system and the proteins in our cells are crucial for regulatory processes and life.One part of this thesis, performed as a part of the EU-founded project AMBIO, deals with the concept of marine biofouling. A number of short peptides have been designed, synthesized, and used to investigate their effect on the settlement on marine biofoulers, such as the Ulva linza algae and the Navicula diatom, on template surfaces coated with thin layers of these molecules. The surfaces have been thoroughly investigated with respect of their physio-chemical properties before and after submersion in artificial seawater and ultimately in suspensions containing the organisms. The most interesting results were obtained with an arginine-rich peptide coating that when introduced to Ulva linza zoospores, displayed extensive settlement, compared to reference surfaces. In addition, a large fraction of the settled spores had an abnormal morphology.The other part of this thesis is focused on designed peptides that when adsorbed on a negatively charged surface adopts a well-defined secondary structure, either α-helical or β-sheet. Precisely placed amino acids in the peptides will strongly disfavor structure in solution, primarily due to electrostatic repulsion, but when the peptides are adsorbed on the negatively charged surfaces, they adopt a well-defined secondary structure due to ion pair bonding. These interactions have been thoroughly investigated by systematic variations of the side-chains. In order to determine the factors contributing to the induced structure, several peptides with different amino acid sequences have been synthesized. Factors that have been investigated include 1) the positive charge density, 2) distribution of positive charges, 3) negative charge density, 4) increasing hydrophobicity, and 5) incorporating amino acids with different helix propensities. Moreover, pH dependence and the effect of different interaction partners have also been investigated. It has also been shown that the system can be modified to incorporate a catalytic site that is only active when the helix is formed. This research will increase our understanding of peptide-surface interactions and might be of importance for both bionanotechnology and medicine.

    Delarbeid
    1. Induction of structure and function in a designed peptide upon adsorption on a silica nanoparticle
    Åpne denne publikasjonen i ny fane eller vindu >>Induction of structure and function in a designed peptide upon adsorption on a silica nanoparticle
    2006 (engelsk)Inngår i: Angewandte Chemie International Edition, ISSN 1433-7851, E-ISSN 1521-3773, Vol. 45, nr 48, s. 8169-8173Artikkel i tidsskrift (Fagfellevurdert) Published
    Abstract [en]

    No abstrack available.

    Emneord
    Amino acids, catalysis, helical structures, nanoparticles, peptides
    HSV kategori
    Identifikatorer
    urn:nbn:se:liu:diva-14548 (URN)10.1002/anie.200600965 (DOI)
    Tilgjengelig fra: 2008-02-25 Laget: 2008-02-25 Sist oppdatert: 2017-12-13bibliografisk kontrollert
    2. Fundamental Design Principles That Guide Induction of Helix upon Formation of Stable Peptide−Nanoparticle Complexes
    Åpne denne publikasjonen i ny fane eller vindu >>Fundamental Design Principles That Guide Induction of Helix upon Formation of Stable Peptide−Nanoparticle Complexes
    2008 (engelsk)Inngår i: Nano letters (Print), ISSN 1530-6984, E-ISSN 1530-6992, Vol. 8, nr 7, s. 1844-1852Artikkel i tidsskrift (Fagfellevurdert) Published
    Abstract [en]

    We have shown that it is possible to design a peptide that has a very low helical content when free in solution but that adopts a well-defined helix when interacting with silica nanoparticles. From a systematic variation of the amino acid composition and distribution in designed peptides, it has been shown that the ability to form helical structure upon binding to the silica surface is dominated by two factors. First, the helical content is strongly correlated with the net positive charge on the side of the helix that interacts with the silica, and arginine residues are strongly favored over lysine residues in these positions. The second important factor is to have a high net negative charge on the side of the helix that faces the solution. Apparently, both attractive and repulsive electrostatic forces dominate the induction and stabilization of a bound helix. It is also evident that using amino acids that have high propensity to form helix in solution are also advantageous for the formation of helix on surfaces.

    HSV kategori
    Identifikatorer
    urn:nbn:se:liu:diva-15015 (URN)10.1021/nl080386s (DOI)
    Tilgjengelig fra: 2008-10-09 Laget: 2008-10-09 Sist oppdatert: 2018-01-12bibliografisk kontrollert
    3. Secondary Structure in de Novo Designed Peptides Induced by Electrostatic Interaction with a Lipid Bilayer Membrane
    Åpne denne publikasjonen i ny fane eller vindu >>Secondary Structure in de Novo Designed Peptides Induced by Electrostatic Interaction with a Lipid Bilayer Membrane
    Vise andre…
    2010 (engelsk)Inngår i: LANGMUIR, ISSN 0743-7463, Vol. 26, nr 9, s. 6437-6448Artikkel i tidsskrift (Fagfellevurdert) Published
    Abstract [en]

    We show that it is possible to induce a defined secondary structure in de nova designed peptides upon electrostatic attachment to negatively charged lipid bilayer vesicles without partitioning of the peptides into the membrane, and that the secondary structure can be varied via small changes in the primary amino acid sequence of the peptides. The peptides have a random-coil conformation in solution, and results from far-UV circular dichroism spectroscopy demonstrate that the structure induced by the interaction with silica nanoparticles is solely alpha-helical and also strongly pH-dependent. The present study shows that negatively charged vesicles, to which the peptides are electrostatically adsorbed via cationic amino acid residues, induce either alpha-helices or beta-sheets and that the conformation is dependent on both lipid composition and variations in peptide primary structure. The pH-dependence of the vesicle-induced peptide secondary structure is weak, which correlates well with small differences in the vesicles electrophoretic mobility, and thus the surface charge, as the pH is varied.

    sted, utgiver, år, opplag, sider
    ACS American Chemical Society, 2010
    HSV kategori
    Identifikatorer
    urn:nbn:se:liu:diva-56297 (URN)10.1021/la100027n (DOI)000276969700056 ()
    Merknad

    The previous status of this article was Manuscript.

    Tilgjengelig fra: 2010-05-07 Laget: 2010-05-07 Sist oppdatert: 2017-01-11
    4. Anomalous settlement behavior of Ulva linza zoospores on cationic oligopeptide surfaces
    Åpne denne publikasjonen i ny fane eller vindu >>Anomalous settlement behavior of Ulva linza zoospores on cationic oligopeptide surfaces
    Vise andre…
    2008 (engelsk)Inngår i: Biofouling (Print), ISSN 0892-7014, E-ISSN 1029-2454, Vol. 24, nr 4, s. 303-312Artikkel i tidsskrift (Fagfellevurdert) Published
    Abstract [en]

    Identification of settlement cues for marine fouling organisms opens up new strategies and methods for biofouling prevention, and enables the development of more effective antifouling materials. To this end, the settlement behaviour of zoospores of the green alga Ulva linza onto cationic oligopeptide self-assembled monolayers (SAMs) has been investigated. The spores interact strongly with lysine- and arginine-rich SAMs, and their settlement appears to be stimulated by these surfaces. Of particular interest is an arginine-rich oligopeptide, which is effective in attracting spores to the surface, but in a way which leaves a large fraction of the settled spores attached to the surface in an anomalous fashion. These 'pseudo-settled' spores are relatively easily detached from the surface and do not undergo the full range of cellular responses associated with normal commitment to settlement. This is a hitherto undocumented mode of settlement, and surface dilution of the arginine-rich peptide with a neutral triglycine peptide demonstrates that both normal and anomalous settlement is proportional to the surface density of the arginine-rich peptide. The settlement experiments are complemented with physical studies of the oligopeptide SAMs, before and after extended immersion in artificial seawater, using infrared spectroscopy, null ellipsometry and contact angle measurements.

    Emneord
    Fouling, algae, self-assembled monolayers, cationic peptides, Ulva, spore
    HSV kategori
    Identifikatorer
    urn:nbn:se:liu:diva-15018 (URN)10.1080/08927010802192650 (DOI)
    Tilgjengelig fra: 2008-10-09 Laget: 2008-10-09 Sist oppdatert: 2017-12-11
    5. Interactions of Zoospores of Ulva linza with Arginine-Rich Oligopeptide Monolayers
    Åpne denne publikasjonen i ny fane eller vindu >>Interactions of Zoospores of Ulva linza with Arginine-Rich Oligopeptide Monolayers
    Vise andre…
    2009 (engelsk)Inngår i: Langmuir, ISSN 0743-7463, E-ISSN 1520-5827, Vol. 25, nr 16, s. 9375-9383Artikkel i tidsskrift (Fagfellevurdert) Published
    Abstract [en]

    We recently reported oil the strong interactions of zoospores of the green alga, Ulva linza with all arginine-rich oligopeptide self-assembled monolayer (SAM) [Biofouling 2008, 24, 303-312], where the arginine-rich peptide induced not only high spore settlement, but also a form of abnormal settlement, or "pseudo-settlement", whereby it proportion of spores do not go through the normal process of surface exploration, adhesive exocytosis, and loss of flagella. Further. it was demonstrated that both the total number of settled spores and the fraction of pseudosettled spores were related to the surface density of the arginine-rich peptide. Here we present a further investigation of the interactions of zoospores of ulva with a set of oligomeric, de nom designed, arginine-rich peptides, specifically aimed to test the effect of peptide primary structure on the interaction. Via variations in the peptide length and by permutations in the amino acid sequences, we gain further insight into the spore-surface interactions. The interpretation of the biological assays is supported by physicochemical characterization of the SAMs using infrared spectroscopy, ellipsometry, and contact angle measurement. Results confirm the importance of arginine residues for the anomalous pseudosettlement, and we found that settlement is modulated by variations in both the total length and peptide primary structure. To elucidate the Causes of the anomalous settlement and the possible relation to peptide-membrane interactions, we also compared the settlement of the "naked" zoospores of Ulva(which present it lipoprotein membrane to the exterior without a discrete polysaccharide cell wall), with the settlement of diatoms (unicellular algae that are surrounded by it silica cell wall), onto the peptide SAMs. Cationic SAMs do not notably affect settlement (attachment), adhesion strength, or viability of diatom cells, Suggesting that the effect of the peptides on zoospores of Ulva is mediated via specific peptide-membrane interactions.

    sted, utgiver, år, opplag, sider
    American Chemical Society (ACS), 2009
    HSV kategori
    Identifikatorer
    urn:nbn:se:liu:diva-19996 (URN)10.1021/la900688g (DOI)
    Merknad

    The previous status of this article was Manuscript.

    Tilgjengelig fra: 2009-08-24 Laget: 2009-08-24 Sist oppdatert: 2017-12-13bibliografisk kontrollert
  • 10.
    Nygren, Patrik
    et al.
    Linköpings universitet, Institutionen för fysik, kemi och biologi, Sensorvetenskap och Molekylfysik. Linköpings universitet, Tekniska högskolan.
    Lundqvist, Martin
    Linköpings universitet, Institutionen för fysik, kemi och biologi, Molekylär Bioteknik. Linköpings universitet, Tekniska högskolan.
    Broo, Klas
    Linköpings universitet, Institutionen för fysik, kemi och biologi. Linköpings universitet, Tekniska högskolan.
    Jonsson, Bengt-Harald
    Linköpings universitet, Institutionen för fysik, kemi och biologi, Molekylär Bioteknik. Linköpings universitet, Tekniska högskolan.
    Fundamental Design Principles That Guide Induction of Helix upon Formation of Stable Peptide−Nanoparticle Complexes2008Inngår i: Nano letters (Print), ISSN 1530-6984, E-ISSN 1530-6992, Vol. 8, nr 7, s. 1844-1852Artikkel i tidsskrift (Fagfellevurdert)
    Abstract [en]

    We have shown that it is possible to design a peptide that has a very low helical content when free in solution but that adopts a well-defined helix when interacting with silica nanoparticles. From a systematic variation of the amino acid composition and distribution in designed peptides, it has been shown that the ability to form helical structure upon binding to the silica surface is dominated by two factors. First, the helical content is strongly correlated with the net positive charge on the side of the helix that interacts with the silica, and arginine residues are strongly favored over lysine residues in these positions. The second important factor is to have a high net negative charge on the side of the helix that faces the solution. Apparently, both attractive and repulsive electrostatic forces dominate the induction and stabilization of a bound helix. It is also evident that using amino acids that have high propensity to form helix in solution are also advantageous for the formation of helix on surfaces.

  • 11.
    Nygren, Patrik
    et al.
    Linköpings universitet, Institutionen för fysik, kemi och biologi, Sensorvetenskap och Molekylfysik. Linköpings universitet, Tekniska högskolan.
    Lundqvist, Martin
    Linköpings universitet, Institutionen för fysik, kemi och biologi, Molekylär Bioteknik. Linköpings universitet, Tekniska högskolan.
    Liedberg, Bo
    Linköpings universitet, Institutionen för fysik, kemi och biologi, Sensorvetenskap och Molekylfysik. Linköpings universitet, Tekniska högskolan.
    Broo, Klas
    Linköpings universitet, Institutionen för fysik, kemi och biologi, Molekylär Bioteknik. Linköpings universitet, Tekniska högskolan.
    Jonsson, Bengt-Harald
    Linköpings universitet, Institutionen för fysik, kemi och biologi, Molekylär Bioteknik. Linköpings universitet, Tekniska högskolan.
    Ederth, Thomas
    Linköpings universitet, Institutionen för fysik, kemi och biologi, Sensorvetenskap och Molekylfysik. Linköpings universitet, Tekniska högskolan.
    Secondary structure in de novo designed peptides induced by electrostatic interaction with particles and membranes.2011Konferansepaper (Annet vitenskapelig)
  • 12.
    Nygren, Patrik
    et al.
    Linköpings universitet, Institutionen för fysik, kemi och biologi, Sensorvetenskap och Molekylfysik. Linköpings universitet, Tekniska högskolan.
    Lundqvist, Martin
    Linköpings universitet, Institutionen för fysik, kemi och biologi, Molekylär Bioteknik. Linköpings universitet, Tekniska högskolan.
    Liedberg, Bo
    Linköpings universitet, Institutionen för fysik, kemi och biologi, Sensorvetenskap och Molekylfysik. Linköpings universitet, Tekniska högskolan.
    Jonsson, Bengt-Harald
    Linköpings universitet, Institutionen för fysik, kemi och biologi, Molekylär Bioteknik. Linköpings universitet, Tekniska högskolan.
    Ederth, Thomas
    Linköpings universitet, Institutionen för fysik, kemi och biologi, Sensorvetenskap och Molekylfysik. Linköpings universitet, Tekniska högskolan.
    Secondary Structure in de Novo Designed Peptides Induced by Electrostatic Interaction with a Lipid Bilayer Membrane2010Inngår i: LANGMUIR, ISSN 0743-7463, Vol. 26, nr 9, s. 6437-6448Artikkel i tidsskrift (Fagfellevurdert)
    Abstract [en]

    We show that it is possible to induce a defined secondary structure in de nova designed peptides upon electrostatic attachment to negatively charged lipid bilayer vesicles without partitioning of the peptides into the membrane, and that the secondary structure can be varied via small changes in the primary amino acid sequence of the peptides. The peptides have a random-coil conformation in solution, and results from far-UV circular dichroism spectroscopy demonstrate that the structure induced by the interaction with silica nanoparticles is solely alpha-helical and also strongly pH-dependent. The present study shows that negatively charged vesicles, to which the peptides are electrostatically adsorbed via cationic amino acid residues, induce either alpha-helices or beta-sheets and that the conformation is dependent on both lipid composition and variations in peptide primary structure. The pH-dependence of the vesicle-induced peptide secondary structure is weak, which correlates well with small differences in the vesicles electrophoretic mobility, and thus the surface charge, as the pH is varied.

  • 13.
    Wetterö, Jonas
    et al.
    Linköpings universitet, Hälsouniversitetet. Linköpings universitet, Institutionen för klinisk och experimentell medicin, Reumatologi.
    Hellerstedt, T.
    Nygren, Patrik
    Linköpings universitet, Tekniska högskolan. Linköpings universitet, Institutionen för fysik, kemi och biologi, Sensorvetenskap och Molekylfysik.
    Broo, K.
    Occupational and Environmental Medicine, Sahlgrenska University Hospital, Göteborg University, Göteborg, Sweden.
    Aili, Daniel
    Linköpings universitet, Tekniska högskolan. Linköpings universitet, Institutionen för fysik, kemi och biologi, Sensorvetenskap och Molekylfysik.
    Liedberg, Bo
    Linköpings universitet, Tekniska högskolan. Linköpings universitet, Institutionen för fysik, kemi och biologi, Sensorvetenskap och Molekylfysik.
    Magnusson, Karl-Eric
    Linköpings universitet, Hälsouniversitetet. Linköpings universitet, Institutionen för klinisk och experimentell medicin, Medicinsk mikrobiologi.
    Immobilized chemoattractant peptides mediate adhesion and distinct calcium-dependent cell signaling in human neutrophils2008Inngår i: Langmuir, ISSN 0743-7463, E-ISSN 1520-5827, Vol. 24, nr 13, s. 6803-6811Artikkel i tidsskrift (Fagfellevurdert)
    Abstract [en]

    Chemotaxis is the stimulated directional migration of cells in response to chemotactic factors, manifested for instance during leukocyte interaction with chemoattractants in inflammation. The N-formyl-Met-Leu-Phe (fMLF) bacterial peptide family is particularly potent in attracting and activating neutrophilic granulocytes. To accomplish defined circumstances for recruitment and activation of cells, we fabricated semitransparent gold-coated glass coverslips functionalized with chemoattractant fMLF receptor peptide agonist analogues. Peptides based on a common leading four-amino-acid sequence Gly-Gly-Gly-Cys were thus coupled to two potent fMLF receptor agonists, N-formyl-Tyr-Nle-Phe-Leu- Nle-Gly-Gly-Gly-Cys and N-formyl-Met-Leu-Phe-Gly-Gly-Gly-Cys, and a formylated control peptide, N-formyl-Gly-Gly-Gly-Cys. They were anchored via the SH group of Cys either directly to the gold surface or a mixed self-assembled monolayer composed of maleimide- and hydroxyl-terminated oligo(ethylene glycol) alkyldisulfides. The overall peptide immobilization procedure was characterized with ellipsometry, contact angle measurement, and infrared spectroscopy. When exposed to granulocytes, the agonist surface rapidly recruited neutrophils and the cells responded with extensive spreading and intracellular calcium transients within minutes. The reference peptide generated no such activation, and the cells maintained a more spherical morphology, suggesting that we have been able to immobilize chemoattractant receptor agonist peptides with retained bioactivity. This is a crucial step in designing surfaces with specific effects on cellular behavior. © 2008 American Chemical Society.

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