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  • 1. Azinas, S.
    et al.
    Bano, F.
    Torca, I.
    Bamford, D. H.
    Schwartz, G. A.
    Esnaola, J.
    Oksanen, H. M.
    Richter, R. P.
    Abrescia, N. G.
    Membrane-containing virus particles exhibit the mechanics of a composite material for genome protection2018Ingår i: Nanoscale, Vol. 10, nr 16, s. 7769-7779Artikel i tidskrift (Refereegranskat)
  • 2.
    Bano, Fouzia
    et al.
    CIC biomaGUNE, Donostia-San Sebastian, Spain.
    Banerji, Suneale
    Howarth, Mark
    Jackson, David G.
    Richter, Ralf P.
    A single molecule assay to probe monovalent and multivalent bonds between hyaluronan and its key leukocyte receptor CD44 under force2016Ingår i: Scientific Reports, E-ISSN 2045-2322, Vol. 6, artikel-id 34176Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Glycosaminoglycans (GAGs), a category of linear, anionic polysaccharides, are ubiquitous in the extracellular space, and important extrinsic regulators of cell function. Despite the recognized significance of mechanical stimuli in cellular communication, however, only few single molecule methods are currently available to study how monovalent and multivalent GAG·protein bonds respond to directed mechanical forces. Here, we have devised such a method, by combining purpose-designed surfaces that afford immobilization of GAGs and receptors at controlled nanoscale organizations with single molecule force spectroscopy (SMFS). We apply the method to study the interaction of the GAG polymer hyaluronan (HA) with CD44, its receptor in vascular endothelium. Individual bonds between HA and CD44 are remarkably resistant to rupture under force in comparison to their low binding affinity. Multiple bonds along a single HA chain rupture sequentially and independently under load. We also demonstrate how strong non-covalent bonds, which are versatile for controlled protein and GAG immobilization, can be effectively used as molecular anchors in SMFS. We thus establish a versatile method for analyzing the nanomechanics of GAG·protein interactions at the level of single GAG chains, which provides new molecular-level insight into the role of mechanical forces in the assembly and function of GAG-rich extracellular matrices.

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  • 3.
    Bano, Fouzia
    et al.
    CIC biomaGUNE, Donostia - San Sebastian, Spain.
    Carril, Mónica
    Di Gianvincenzo, Paolo
    Richter, Ralf P.
    Interaction of hyaluronan with cationic nanoparticles2015Ingår i: Langmuir, ISSN 0743-7463, E-ISSN 1520-5827, Vol. 31, nr 30, s. 8411-8420Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    The polysaccharide hyaluronan (HA) is a main component of peri- and extracellular matrix, and an attractive molecule for materials design in tissue engineering and nanomedicine. Here, we study the morphology of complexes that form upon interaction of nanometer-sized amine-coated gold particles with this anionic, linear, and regular biopolymer in solution and grafted to a surface. We find that cationic nanoparticles (NPs) have profound effects on HA morphology on the molecular and supramolecular scale. Quartz crystal microbalance (QCM-D) shows that depending on their relative abundance, cationic NPs promote either strong compaction or swelling of films of surface-grafted HA polymers (HA brushes). Transmission electron and atomic force microscopy reveal that the NPs do also give rise to complexes of distinct morphologies–compact nanoscopic spheres and extended microscopic fibers–upon interaction with HA polymers in solution. In particular, stable and hydrated spherical complexes of single HA polymers with NPs can be prepared when balancing the ionizable groups on HA and NPs. The observed self-assembly phenomena could be useful for the design of drug delivery vehicles and a better understanding of the reorganization of HA-rich synthetic or biological matrices.

  • 4.
    Bano, Fouzia
    et al.
    ELETTRA, Sincrotrone Trieste; Scuola Internazionale Superiore di Studi Avanzati (SISSA).
    Fruk, Ljiljana
    Sanavio, Barbara
    Glettenberg, Maximilian
    Casalis, Loredana
    Niemeyer, Christof M.
    Scoles, Giacinto
    Toward multiprotein nanoarrays using nanografting and DNA directed immobilization of proteins2009Ingår i: Nano Letters, ISSN 1530-6984, E-ISSN 1530-6992, Vol. 9, nr 7, s. 2614-2618Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Atomic force microscopy nanografting was utilized to prepare DNA nanopatches of different sizes (200 × 200 to 1000 × 1000 nm2) onto which DNA−protein conjugates can be anchored through DNA-directed immobilization. Height measurements were used to assess the binding of the proteins as well as their subsequent interaction with other components, such as antibodies. The results indicate that nanografted patch arrays are well suited for application in biosensing and could enable the fabrication of multifeature protein nanoarrays.

  • 5.
    Bano, Fouzia
    et al.
    University of Liège, Department of Chemistry, Belgium.
    Sluysmans, D.
    Wislez, A.
    Duwez, A. -S
    Unraveling the complexity of the interactions of DNA nucleotides with gold by single molecule force spectroscopy2015Ingår i: Nanoscale, ISSN 2040-3364, E-ISSN 2040-3372, Vol. 7, nr 46, s. 19528-19533Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Addressing the effect of different environmental factors on the adsorption of DNA to solid supports is critical for the development of robust miniaturized devices for applications ranging from biosensors to next generation molecular technology. Most of the time, thiol-based chemistry is used to anchor DNA on gold – a substrate commonly used in nanotechnology – and little is known about the direct interaction between DNA and gold. So far there have been no systematic studies on the direct adsorption behavior of the deoxyribonucleotides (i.e., a nitrogenous base, a deoxyribose sugar, and a phosphate group) and on the factors that govern the DNA–gold bond strength. Here, using single molecule force spectroscopy, we investigated the interaction of the four individual nucleotides, adenine, guanine, cytosine, and thymine, with gold. Experiments were performed in three salinity conditions and two surface dwell times to reveal the factors that influence nucleotide–Au bond strength. Force data show that, at physiological ionic strength, adenine–Au interactions are stronger, asymmetrical and independent of surface dwell time as compared to cytosine–Au and guanine–Au interactions. We suggest that in these conditions only adenine is able to chemisorb on gold. A decrease of the ionic strength significantly increases the bond strength for all nucleotides. We show that moderate ionic strength along with longer surface dwell period suggest weak chemisorption also for cytosine and guanine.

  • 6.
    Bano, Fouzia
    et al.
    School of Biomedical Sciences, Faculty of Biological Sciences, School of Physics and Astronomy, Faculty of Mathematics and Physical Sciences, and Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, United Kingdom; CIC biomaGUNE, Biosurfaces Laboratory, Donostia-San Sebastian, Spain.
    Tammi, M. I.
    Kang, D. W.
    Harris, E. N.
    Richter, R. P.
    Single-molecule unbinding forces between the polysaccharide hyaluronan and its binding proteins2018Ingår i: Biophysical Journal, ISSN 0006-3495, E-ISSN 1542-0086, Vol. 114, nr 12, s. 2910-2922Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    The extracellular polysaccharide hyaluronan (HA) is ubiquitous in all vertebrate tissues, where its various functions are encoded in the supramolecular complexes and matrices that it forms with HA-binding proteins (hyaladherins). In tissues, these supramolecular architectures are frequently subjected to mechanical stress, yet how this affects the intermolecular bonding is largely unknown. Here, we used a recently developed single-molecule force spectroscopy platform to analyze and compare the mechanical strength of bonds between HA and a panel of hyaladherins from the Link module superfamily, namely the complex of the proteoglycan aggrecan and cartilage link protein, the proteoglycan versican, the inflammation-associated protein TSG-6, the HA receptor for endocytosis (stabilin-2/HARE), and the HA receptor CD44. We find that the resistance to tensile stress for these hyaladherins correlates with the size of the HA-binding domain. The lowest mean rupture forces are observed for members of the type A subgroup (i.e., with the shortest HA-binding domains; TSG-6 and HARE). In contrast, the mechanical stability of the bond formed by aggrecan in complex with cartilage link protein (two members of the type C subgroup, i.e., with the longest HA-binding domains) and HA is equal or even superior to the high affinity streptavidin⋅biotin bond. Implications for the molecular mechanism of unbinding of HA⋅hyaladherin bonds under force are discussed, which underpin the mechanical properties of HA⋅hyaladherin complexes and HA-rich extracellular matrices.

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  • 7. Bar, Laure
    et al.
    Dejeu, Jérôme
    Lartia, Rémy
    Bano, Fouzia
    Richter, Ralf P.
    Coche-Guérente, Liliane
    Boturyn, Didier
    Impact of antigen density on recognition by monoclonal antibodies2020Ingår i: Analytical Biochemistry, ISSN 0003-2697, E-ISSN 1096-0309, Vol. 92, nr 7, s. 5396-5403Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Understanding antigen–antibody interactions is important to many emerging medical and bioanalytical applications. In particular, the levels of antigen expression at the cell surface may determine antibody-mediated cell death. This parameter has a clear effect on outcome in patients undergoing immunotherapy. In this context, CD20 which is expressed in the membrane of B cells has received significant attention as target for immunotherapy of leukemia and lymphoma using the monoclonal antibody rituximab. To systematically study the impact of CD20 density on antibody recognition, we designed self-assembled monolayers that display tunable CD20 epitope densities. For this purpose, we developed in situ click chemistry to functionalize SPR sensor chips. We find that the rituximab binding affinity depends sensitively and nonmonotonously on CD20 surface density. Strongest binding, with an equilibrium dissociation constant (KD = 32 nM) close to values previously reported from in vitro analysis with B cells (apparent KD between 5 and 19 nM), was obtained for an average inter-antigen spacing of 2 nm. This distance is required for improving rituximab recognition, and in agreement with the known requirement of CD20 to form clusters to elicit a biological response. More generally, this study offers an interesting outlook in the understanding of the necessity of epitope clusters for effective mAb recognition.

  • 8. Bosco, Alessandro
    et al.
    Bano, Fouzia
    Scuola Internazionale Superiore di Studi Avanzati (SISSA), Trieste, Italy; NanoChemistry and Molecular Systems Department of Chemistry, University of Liège,Liège, Belgium.
    Parisse, Pietro
    Casalis, Loredana
    DeSimone, Antonio
    Micheletti, Cristian
    Hybridization in nanostructured DNA monolayers probed by AFM: theory versus experiment2012Ingår i: Nanoscale, ISSN 2040-3364, E-ISSN 2040-3372, Vol. 4, nr 5, s. 1734-1741Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Nanografted monolayers (NAMs) of DNA show novel physico-chemical properties that make them ideally suited for advanced biosensing applications. In comparison with alternative solid-phase techniques for diagnostic DNA detection, NAMs have the advantage of combining a small size with a high homogeneity of the DNA surface coverage. These two properties favour the extreme miniaturization and ultrasensitivity in high-throughput biosensing devices. The systematic use of NAMs for quantitative DNA (and protein) detection has so far suffered from the lack of a control on key fabrication parameters, such as the ss- or ds-DNA surface coverage. Here we report on a combined experimental–computational study that allows us to estimate the surface density of the grafted DNA by analyzing the sample mechanical response, that is the DNA patch height vs. applied tip load curves. It is shown that the same analysis scheme can be used to detect the occurrence of hybridization with complementary strands in solution and estimate its efficiency. Thanks to these quantitative relationships it is possible to use a single AFM-based setup to: (i) fabricate a DNA NAM, (ii) control the DNA surface coverage, and (iii) characterize its level of hybridization helping the design of NAMs with pre-determined fabrication parameters.

  • 9. Castronovo, Matteo
    et al.
    Bano, Fouzia
    Elettra Synchrotron Laboratory, Basovizza, Trieste, Italy; International School for Advanced Studies, Trieste, Italy.
    Raugei, Simone
    Scaini, Denis
    Dell’Angela, Martina
    Hudej, Robert
    Casalis, Loredana
    Scoles, Giacinto
    Mechanical stabilization effect of water on a membrane-like system2007Ingår i: Journal of the American Chemical Society, ISSN 0002-7863, E-ISSN 1520-5126, Vol. 129, nr 9, s. 2636-2641Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    The penetration resistance of a prototypical model-membrane system (HS−(CH2)11−OH self-assembled monolayer (SAM) on Au(111)) to the tip of an atomic force microscope (AFM) is investigated in the presence of different solvents. The compressibility (i.e., height vs tip load) of the HS−(CH2)11−OH SAM is studied differentially, with respect to a reference structure. The reference consists of hydrophobic alkylthiol molecules (HS−(CH2)17−CH3) embedded as nanosized patches into the hydrophilic SAM by nanografting, an AFM-assisted nanolithography technique. We find that the penetration resistance of the hydrophilic SAM depends on the nature of the solvent and is much higher in the presence of water than in 2-butanol. In contrast, no solvent-dependent effect is observed in the case of hydrophobic SAMs. We argue that the mechanical resistance of the hydroxyl-terminated SAM is a consequence of the structural order of the solvent−SAM interface, as suggested by our molecular dynamics simulations. The simulations show that in the presence of 2-butanol the polar head groups of the HS−(CH2)11−OH SAM, which bind only weakly to the solvent molecules, try to bind to each other, disrupting the local order at the interface. On the contrary, in the presence of water the polar head groups bind preferentially to the solvent that, in turn, mediates the release of the surface strain, leading to a more ordered interface. We suggest that the mechanical stabilization effect induced by water may be responsible for the stability of even more complex, real membrane systems.

  • 10. Frost, Rickard
    et al.
    Débarre, Delphine
    Jana, Saikat
    Bano, Fouzia
    School of Biomedical Sciences, Faculty ofBiological Sciences, School of Physics and Astronomy, Faculty ofEngineering and Physical Sciences, Astbury Centre of StructuralMolecular Biology, and Bragg Centre for Materials Research,University of Leeds, Leeds LS2 9JT, United Kingdom.
    Schünemann, Jürgen
    Görlich, Dirk
    Richter, Ralf P.
    A method to quantify molecular diffusion within thin solvated polymer films: A case study on films of natively unfolded nucleoporins2020Ingår i: ACS Nano, ISSN 1936-0851, E-ISSN 1936-086X, Vol. 14, nr 8, s. 9938-9952Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    We present a method to probe molecular and nanoparticle diffusion within thin, solvated polymer coatings. The device exploits the confinement with well-defined geometry that forms at the interface between a planar and a hemispherical surface (of which at least one is coated with polymers) in close contact and uses this confinement to analyze diffusion processes without interference of exchange with and diffusion in the bulk solution. With this method, which we call plane–sphere confinement microscopy (PSCM), information regarding the partitioning of molecules between the polymer coating and the bulk liquid is also obtained. Thanks to the shape of the confined geometry, diffusion and partitioning can be mapped as a function of compression and concentration of the coating in a single experiment. The method is versatile and can be integrated with conventional optical microscopes; thus it should find widespread use in the many application areas exploiting functional polymer coatings. We demonstrate the use of PSCM using brushes of natively unfolded nucleoporin domains rich in phenylalanine–glycine repeats (FG domains). A meshwork of FG domains is known to be responsible for the selective transport of nuclear transport receptors (NTRs) and their macromolecular cargos across the nuclear envelope that separates the cytosol and the nucleus of living cells. We find that the selectivity of NTR uptake by FG domain films depends sensitively on FG domain concentration and that the interaction of NTRs with FG domains obstructs NTR movement only moderately. These observations contribute important information to better understand the mechanisms of selective NTR transport.

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  • 11. Giubertoni, Giulia
    et al.
    Ortíz, Alberto Pérez de Alba
    Bano, Fouzia
    School of Biomedical Sciences, Faculty of Biological Sciences, School of Physics and Astronomy, Faculty of Engineering and Physical Sciences, Astbury Centre of Structural Molecular Biology, and Bragg Centre for Materials Research, University of Leeds, Leeds, UK.
    Zhang, Xing
    Linhardt, Robert J.
    Green, Dixy E.
    DeAngelis, Paul L.
    Koenderink, Gijsje H.
    Richter, Ralf P.
    Ensing, Bernd
    Bakker, Huib J.
    Strong reduction of the chain rigidity of hyaluronan by selective binding of Ca2+ ions2021Ingår i: Macromolecules, ISSN 0024-9297, E-ISSN 1520-5835, Vol. 54, nr 3, s. 1137-1146Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    The biological functions of natural polyelectrolytes are strongly influenced by the presence of ions, which bind to the polymer chains and thereby modify their properties. Although the biological impact of such modifications is well recognized, a detailed molecular picture of the binding process and of the mechanisms that drive the subsequent structural changes in the polymer is lacking. Here, we study the molecular mechanism of the condensation of calcium, a divalent cation, on hyaluronan, a ubiquitous polymer in human tissues. By combining two-dimensional infrared spectroscopy experiments with molecular dynamics simulations, we find that calcium specifically binds to hyaluronan at millimolar concentrations. Because of its large size and charge, the calcium cation can bind simultaneously to the negatively charged carboxylate group and the amide group of adjacent saccharide units. Molecular dynamics simulations and single-chain force spectroscopy measurements provide evidence that the binding of the calcium ions weakens the intramolecular hydrogen-bond network of hyaluronan, increasing the flexibility of the polymer chain. We also observe that the binding of calcium to hyaluronan saturates at a maximum binding fraction of ∼10–15 mol %. This saturation indicates that the binding of Ca2+ strongly reduces the probability of subsequent binding of Ca2+ at neighboring binding sites, possibly as a result of enhanced conformational fluctuations and/or electrostatic repulsion effects. Our findings provide a detailed molecular picture of ion condensation and reveal the severe effect of a few, selective and localized electrostatic interactions on the rigidity of a polyelectrolyte chain.

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  • 12.
    Herrero, M. Antonia
    et al.
    Center of Excellence for Nanostructured Materials, Department of Pharmaceutical Sciences, and INSTM, University of Trieste, Piazzale Europa 1, 34127 Trieste, Italy, Departamento de Química Orgánica, Facultad de Química, Universidad de Castilla-La Mancha, 13071 Ciudad Real, Spain, SISSA, 34014 Trieste, Italy, Nanomedicine Laboratory, Centre for Drug Delivery Research, The School of Pharmacy, University of London, London WC1N 1AX, U.K., CNRS, Institut de Biologie Moléculaire et Cellulaire, UPR9021....
    Toma, Francesca M.
    Center of Excellence for Nanostructured Materials, Department of Pharmaceutical Sciences, and INSTM, University of Trieste, Piazzale Europa 1, 34127 Trieste, Italy, Departamento de Química Orgánica, Facultad de Química, Universidad de Castilla-La Mancha, 13071 Ciudad Real, Spain, SISSA, 34014 Trieste, Italy, Nanomedicine Laboratory, Centre for Drug Delivery Research, The School of Pharmacy, University of London, London WC1N 1AX, U.K., CNRS, Institut de Biologie Moléculaire et Cellulaire, UPR9021....
    Al-Jamal, Khuloud T.
    Center of Excellence for Nanostructured Materials, Department of Pharmaceutical Sciences, and INSTM, University of Trieste, Piazzale Europa 1, 34127 Trieste, Italy, Departamento de Química Orgánica, Facultad de Química, Universidad de Castilla-La Mancha, 13071 Ciudad Real, Spain, SISSA, 34014 Trieste, Italy, Nanomedicine Laboratory, Centre for Drug Delivery Research, The School of Pharmacy, University of London, London WC1N 1AX, U.K., CNRS, Institut de Biologie Moléculaire et Cellulaire, UPR9021....
    Kostarelos, Kostas
    Center of Excellence for Nanostructured Materials, Department of Pharmaceutical Sciences, and INSTM, University of Trieste, Piazzale Europa 1, 34127 Trieste, Italy, Departamento de Química Orgánica, Facultad de Química, Universidad de Castilla-La Mancha, 13071 Ciudad Real, Spain, SISSA, 34014 Trieste, Italy, Nanomedicine Laboratory, Centre for Drug Delivery Research, The School of Pharmacy, University of London, London WC1N 1AX, U.K., CNRS, Institut de Biologie Moléculaire et Cellulaire, UPR9021....
    Bianco, Alberto
    Center of Excellence for Nanostructured Materials, Department of Pharmaceutical Sciences, and INSTM, University of Trieste, Piazzale Europa 1, 34127 Trieste, Italy, Departamento de Química Orgánica, Facultad de Química, Universidad de Castilla-La Mancha, 13071 Ciudad Real, Spain, SISSA, 34014 Trieste, Italy, Nanomedicine Laboratory, Centre for Drug Delivery Research, The School of Pharmacy, University of London, London WC1N 1AX, U.K., CNRS, Institut de Biologie Moléculaire et Cellulaire, UPR9021....
    Da Ros, Tatiana
    Center of Excellence for Nanostructured Materials, Department of Pharmaceutical Sciences, and INSTM, University of Trieste, Piazzale Europa 1, 34127 Trieste, Italy, Departamento de Química Orgánica, Facultad de Química, Universidad de Castilla-La Mancha, 13071 Ciudad Real, Spain, SISSA, 34014 Trieste, Italy, Nanomedicine Laboratory, Centre for Drug Delivery Research, The School of Pharmacy, University of London, London WC1N 1AX, U.K., CNRS, Institut de Biologie Moléculaire et Cellulaire, UPR9021....
    Bano, Fouzia
    Center of Excellence for Nanostructured Materials, Department of Pharmaceutical Sciences, and INSTM, University of Trieste, Piazzale Europa 1, 34127 Trieste, Italy, Departamento de Química Orgánica, Facultad de Química, Universidad de Castilla-La Mancha, 13071 Ciudad Real, Spain, SISSA, 34014 Trieste, Italy, Nanomedicine Laboratory, Centre for Drug Delivery Research, The School of Pharmacy, University of London, London WC1N 1AX, U.K., CNRS, Institut de Biologie Moléculaire et Cellulaire, UPR9021....
    Casalis, Loredana
    Center of Excellence for Nanostructured Materials, Department of Pharmaceutical Sciences, and INSTM, University of Trieste, Piazzale Europa 1, 34127 Trieste, Italy, Departamento de Química Orgánica, Facultad de Química, Universidad de Castilla-La Mancha, 13071 Ciudad Real, Spain, SISSA, 34014 Trieste, Italy, Nanomedicine Laboratory, Centre for Drug Delivery Research, The School of Pharmacy, University of London, London WC1N 1AX, U.K., CNRS, Institut de Biologie Moléculaire et Cellulaire, UPR9021....
    Scoles, Giacinto
    Center of Excellence for Nanostructured Materials, Department of Pharmaceutical Sciences, and INSTM, University of Trieste, Piazzale Europa 1, 34127 Trieste, Italy, Departamento de Química Orgánica, Facultad de Química, Universidad de Castilla-La Mancha, 13071 Ciudad Real, Spain, SISSA, 34014 Trieste, Italy, Nanomedicine Laboratory, Centre for Drug Delivery Research, The School of Pharmacy, University of London, London WC1N 1AX, U.K., CNRS, Institut de Biologie Moléculaire et Cellulaire, UPR9021....
    Prato, Maurizio
    Center of Excellence for Nanostructured Materials, Department of Pharmaceutical Sciences, and INSTM, University of Trieste, Piazzale Europa 1, 34127 Trieste, Italy, Departamento de Química Orgánica, Facultad de Química, Universidad de Castilla-La Mancha, 13071 Ciudad Real, Spain, SISSA, 34014 Trieste, Italy, Nanomedicine Laboratory, Centre for Drug Delivery Research, The School of Pharmacy, University of London, London WC1N 1AX, U.K., CNRS, Institut de Biologie Moléculaire et Cellulaire, UPR9021....
    Synthesis and characterization of a carbon nanotube−dendron series for efficient sirna delivery2009Ingår i: Journal of the American Chemical Society, ISSN 0002-7863, E-ISSN 1520-5126, Vol. 131, nr 28, s. 9843-9848Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    A new series of dendron-functionalized multiwalled carbon nanotube (MWNT) derivatives, characterized by the presence of numerous positively charged tetraalkyl ammonium salts at the periphery of the dendron, has been synthesized. The positive charges on the MWNT surface, coupled with the unique ability of carbon nanotubes (CNTs) to penetrate cell membranes, make the new derivatives potentially ideal vectors for siRNA delivery. Using a fluorescently labeled, noncoding siRNA sequence, we demonstrate that cytoplasmic delivery of the nucleic acid is remarkably increased throughout the different dendron generations. The work reported here highlights the fact that dendron-functionalized CNTs can be rationally designed as efficient carriers of siRNA that can eventually lead to gene silencing.

  • 13. Heudt, Laetitia
    et al.
    Debois, Delphine
    Zimmerman, Tyler A.
    Köhler, Laurent
    Bano, Fouzia
    Department of Chemistry, Nanochemistry and Molecular Systems, University of Liege, Liège, Belgium.
    Partouche, Franck
    Duwez, Anne-Sophie
    Gilbert, Bernard
    De Pauw, Edwin
    Raman spectroscopy and laser desorption mass spectrometry for minimal destructive forensic analysis of black and color inkjet printed documents2012Ingår i: Forensic Science International, ISSN 0379-0738, E-ISSN 1872-6283, Vol. 219, nr 1-3, s. 64-75Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Inkjet ink analysis is the best way to discriminate between printed documents, or even though more difficult, to connect an inkjet printed document with a brand or model of printers. Raman spectroscopy and laser desorption mass spectrometry (LDMS) have been demonstrated as powerful tools for dyes and pigments analysis, which are ink components. The aim of this work is to evaluate the aforementioned techniques for inkjet inks analysis in terms of discriminating power, information quality, and nondestructive capability. So, we investigated 10 different inkjet ink cartridges (primary colors and black), 7 from the HP manufacturer and one each from Epson, Canon and Lexmark. This paper demonstrates the capabilities of three methods: Raman spectroscopy, LDMS and MALDI-MS. Raman spectroscopy, as it is preferable to try the nondestructive approach first, is successfully adapted to the analysis of color printed documents in most cases. For analysis of color inkjet inks by LDMS, we show that a MALDI matrix (9-aminoacridine, 9AA) is needed to desorb and to ionize dyes from most inkjet inks (except Epson inks). Therefore, a method was developed to apply the 9AA MALDI matrix directly onto the piece of paper while avoiding analyte spreading. The obtained mass spectra are very discriminating and lead to information about ink additives and paper compositions. Discrimination of black inkjet printed documents is more difficult because of the common use of carbon black as the principal pigment. We show for the first time the possibility to discriminate between two black-printed documents coming from different, as well as from the same, manufacturers. Mass spectra recorded from black inks in positive ion mode LDMS detect polyethylene glycol polymers which have characteristic mass distributions and end groups. Moreover, software has been developed for rapid and objective comparison of the low mass range of these positive mode LDMS spectra which have characteristic unknown peaks.

  • 14. Mirmomtaz, Elham
    et al.
    Castronovo, Matteo
    Grunwald, Christian
    Bano, Fouzia
    ELETTRA, Sincrotrone Trieste S.C.p.A; Scuola Internazionale Superiore di Studi Avanzati (SISSA).
    Scaini, Denis
    Ensafi, Ali A.
    Scoles, Giacinto
    Casalis, Loredana
    Quantitative study of the effect of coverage on the hybridization efficiency of surface-bound DNA nanostructures2008Ingår i: Nano Letters, ISSN 1530-6984, E-ISSN 1530-6992, Vol. 8, nr 12, s. 4134-4139Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    We demonstrate that, contrary to current understanding, the density of probe molecules is not responsible for the lack of hybridization in high density single-stranded DNA (ss-DNA) self-assembled monolayers (SAMs). To this end, we use nanografting to fabricate well packed ss-DNA nanopatches within a “carpet matrix” SAM of inert thiols on gold surfaces. The DNA surface density is varied by changing the “writing” parameters, for example, tip speed, and number of scan lines. Since ss-DNA is 50 times more flexible than ds-DNA, hybridization leads to a transition to a “standing up” phase. Therefore, accurate height and compressibility measurements of the nanopatches before and after hybridization allow reliable, sensitive, and label-free detection of hybridization. Side-by-side comparison of self-assembled and nanografted DNA-monolayers shows that the latter, while denser than the former, display higher hybridization efficiencies.

  • 15.
    Nadeem, Aftab
    et al.
    Umeå universitet, Medicinska fakulteten, Institutionen för molekylärbiologi (Medicinska fakulteten). Umeå universitet, Medicinska fakulteten, Umeå Centre for Microbial Research (UCMR). Umeå universitet, Medicinska fakulteten, Molekylär Infektionsmedicin, Sverige (MIMS).
    Nagampalli, Raghavendra
    Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Kemiska institutionen. Umeå universitet, Medicinska fakulteten, Umeå Centre for Microbial Research (UCMR).
    Toh, Eric
    Umeå universitet, Medicinska fakulteten, Umeå Centre for Microbial Research (UCMR). Umeå universitet, Medicinska fakulteten, Institutionen för molekylärbiologi (Medicinska fakulteten). Umeå universitet, Medicinska fakulteten, Molekylär Infektionsmedicin, Sverige (MIMS).
    Alam, Athar
    Umeå universitet, Medicinska fakulteten, Institutionen för klinisk mikrobiologi. Umeå universitet, Medicinska fakulteten, Umeå Centre for Microbial Research (UCMR).
    Myint, Si Lhyam
    Umeå universitet, Medicinska fakulteten, Molekylär Infektionsmedicin, Sverige (MIMS). Umeå universitet, Medicinska fakulteten, Institutionen för molekylärbiologi (Medicinska fakulteten). Umeå universitet, Medicinska fakulteten, Umeå Centre for Microbial Research (UCMR).
    Heidler, Thomas
    Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Kemiska institutionen. Umeå universitet, Medicinska fakulteten, Umeå Centre for Microbial Research (UCMR).
    Dongre, Mitesh
    Umeå universitet, Medicinska fakulteten, Institutionen för molekylärbiologi (Medicinska fakulteten). Umeå universitet, Medicinska fakulteten, Molekylär Infektionsmedicin, Sverige (MIMS). Umeå universitet, Medicinska fakulteten, Umeå Centre for Microbial Research (UCMR).
    Zlatkov, Nikola
    Umeå universitet, Medicinska fakulteten, Institutionen för molekylärbiologi (Medicinska fakulteten). Umeå universitet, Medicinska fakulteten, Molekylär Infektionsmedicin, Sverige (MIMS). Umeå universitet, Medicinska fakulteten, Umeå Centre for Microbial Research (UCMR).
    Pace, Hudson
    Umeå universitet, Medicinska fakulteten, Umeå Centre for Microbial Research (UCMR). Umeå universitet, Medicinska fakulteten, Institutionen för klinisk mikrobiologi. Umeå universitet, Medicinska fakulteten, Wallenberg centrum för molekylär medicin vid Umeå universitet (WCMM).
    Bano, Fouzia
    Umeå universitet, Medicinska fakulteten, Institutionen för klinisk mikrobiologi. Umeå universitet, Medicinska fakulteten, Wallenberg centrum för molekylär medicin vid Umeå universitet (WCMM). Umeå universitet, Medicinska fakulteten, Umeå Centre for Microbial Research (UCMR).
    Sjöstedt, Anders
    Umeå universitet, Medicinska fakulteten, Institutionen för klinisk mikrobiologi. Umeå universitet, Medicinska fakulteten, Umeå Centre for Microbial Research (UCMR).
    Bally, Marta
    Umeå universitet, Medicinska fakulteten, Institutionen för klinisk mikrobiologi. Umeå universitet, Medicinska fakulteten, Wallenberg centrum för molekylär medicin vid Umeå universitet (WCMM). Umeå universitet, Medicinska fakulteten, Umeå Centre for Microbial Research (UCMR).
    Uhlin, Bernt Eric
    Umeå universitet, Medicinska fakulteten, Umeå Centre for Microbial Research (UCMR). Umeå universitet, Medicinska fakulteten, Molekylär Infektionsmedicin, Sverige (MIMS). Umeå universitet, Medicinska fakulteten, Institutionen för molekylärbiologi (Medicinska fakulteten).
    Wai, Sun Nyunt
    Umeå universitet, Medicinska fakulteten, Institutionen för molekylärbiologi (Medicinska fakulteten). Umeå universitet, Medicinska fakulteten, Umeå Centre for Microbial Research (UCMR). Umeå universitet, Medicinska fakulteten, Molekylär Infektionsmedicin, Sverige (MIMS).
    Persson, Karina
    Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Kemiska institutionen. Umeå universitet, Medicinska fakulteten, Umeå Centre for Microbial Research (UCMR).
    A tripartite cytolytic toxin formed by Vibrio cholerae proteins with flagellum-facilitated secretion2021Ingår i: Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, E-ISSN 1091-6490, Vol. 118, nr 47, artikel-id e2111418118Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Vibrio cholerae, responsible for outbreaks of cholera disease, is a highly motile organism by virtue of a single flagellum. We describe how the flagellum facilitates the secretion of three V. cholerae proteins encoded by a hitherto-unrecognized genomic island. The proteins MakA/B/E can form a tripartite toxin that lyses erythrocytes and is cytotoxic to cultured human cells. A structural basis for the cytolytic activity of the Mak proteins was obtained by X-ray crystallography. Flagellum-facilitated secretion ensuring spatially coordinated delivery of Mak proteins revealed a role for the V. cholerae flagellum considered of particular significance for the bacterial environmental persistence. Our findings will pave the way for the development of diagnostics and therapeutic strategies against pathogenic Vibrionaceae.

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  • 16.
    Prittinen, Juha
    et al.
    Umeå universitet, Medicinska fakulteten, Institutionen för integrativ medicinsk biologi (IMB).
    Zhou, Xin
    Umeå universitet, Medicinska fakulteten, Institutionen för integrativ medicinsk biologi (IMB).
    Bano, Fouzia
    Umeå universitet, Medicinska fakulteten, Institutionen för klinisk mikrobiologi. Umeå universitet, Medicinska fakulteten, Wallenberg centrum för molekylär medicin vid Umeå universitet (WCMM).
    Backman, Ludvig J.
    Umeå universitet, Medicinska fakulteten, Institutionen för integrativ medicinsk biologi (IMB). Umeå universitet, Medicinska fakulteten, Institutionen för samhällsmedicin och rehabilitering.
    Danielson, Patrik
    Umeå universitet, Medicinska fakulteten, Institutionen för integrativ medicinsk biologi (IMB). Umeå universitet, Medicinska fakulteten, Institutionen för klinisk vetenskap, Oftalmiatrik.
    Microstructured collagen films for 3D corneal stroma modelling2022Ingår i: Connective Tissue Research, ISSN 0300-8207, E-ISSN 1607-8438, Vol. 63, nr 5, s. 443-452Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Purpose/aim: Corneal injury is a major cause of impaired vision around the globe. The fine structure of the corneal stroma plays a pivotal role in the phenotype and behavior of the embedded cells during homeostasis and healing after trauma or infection. In order to study healing processes in the cornea, it is important to create culture systems that functionally mimic the natural environment.

    Materials and methods: Collagen solution was vitrified on top of a grated film to achieve thin collagen films with parallel microgrooves. Keratocytes (corneal stromal cells) were cultured on the films either as a single layer or as stacked layers of films and cells. SEM and F-actin staining were used to analyze the pattern transference onto the collagen and the cell orientation on the films. Cell viability was analyzed with MTS and live/dead staining. Keratocytes, fibroblasts, and myofibroblasts were cultured to study the pattern’s effect on phenotype.

    Results: A microstructured collagen film-based culture system that guides keratocytes (stromal cells) to their native, layerwise perpendicular orientation in 3D and that can support fibroblasts and myofibroblasts was created. The films are thin and transparent enough to observe cells at least three layers deep. The cells maintain viability in 2D and 3D cultures and the films can support fibroblast and myofibroblast phenotypes.

    Conclusions: The films provide an easily reproducible stroma model that maintains high cell viability and improves the preservation of the keratocyte phenotype in keratocytes that are differentiated to fibroblasts.

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  • 17. Szuba, Agata
    et al.
    Bano, Fouzia
    School of Biomedical Sciences, Faculty of Biological Sciences, Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, United Kingdom; School of Physics and Astronomy, Faculty of Engineering and Physical Sciences, University of Leeds, Leeds, United Kingdom; Bragg Centre for Materials Research, University of Leeds, Leeds, United Kingdom.
    Linares, Gerard Castro
    Iv, Francois
    Mavrakis, Manos
    Richter, Ralf P.
    Bertin, Aurélie
    Koenderink, Gijsje H.
    Membrane binding controls ordered self-assembly of animal septins2021Ingår i: eLIFE, E-ISSN 2050-084X, Vol. 10, artikel-id e63349Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Septins are conserved cytoskeletal proteins that regulate cell cortex mechanics. The mechanisms of their interactions with the plasma membrane remain poorly understood. Here, we show by cell-free reconstitution that binding to flat lipid membranes requires electrostatic interactions of septins with anionic lipids and promotes the ordered self-assembly of fly septins into filamentous meshworks. Transmission electron microscopy reveals that both fly and mammalian septin hexamers form arrays of single and paired filaments. Atomic force microscopy and quartz crystal microbalance demonstrate that the fly filaments form mechanically rigid, 12- to 18-nm thick, double layers of septins. By contrast, C-terminally truncated septin mutants form 4-nm thin monolayers, indicating that stacking requires the C-terminal coiled coils on DSep2 and Pnut subunits. Our work shows that membrane binding is required for fly septins to form ordered arrays of single and paired filaments and provides new insights into the mechanisms by which septins may regulate cell surface mechanics.

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  • 18. Wislez, Arnaud
    et al.
    Sluysmans, Damien
    Giamblanco, Nicoletta
    Willet, Nicolas
    Bano, Fouzia
    Weerdt, Cécile Van De
    Detrembleur, Christophe
    Duwez, Anne-Sophie
    How to Increase Adhesion Strength of Catechol Polymers to Wet Inorganic Surfaces2020Ingår i: Biomacromolecules, Vol. 22, nr 1, s. 183-189Artikel i tidskrift (Refereegranskat)
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