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Wyszukujesz frazę "82.37.Rs" wg kryterium: Temat

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    Wyświetlanie 1-5 z 5
    Tytuł:
    Force Spectroscopy of Polyclonal and Monoclonal Anti-Bovine Serum Albumin Antibodies - BSA Complexes
    Autorzy:
    Chtcheglova, L. A.
    Dietler, G.
    Powiązania:
    https://bibliotekanauki.pl/articles/2036898.pdf
    Data publikacji:
    2003
    Wydawca:
    Polska Akademia Nauk. Instytut Fizyki PAN
    Tematy:
    82.37.Gk
    82.37.Rs
    Opis:
    The specific interactions between bovine serum albumin and poly- or two monoclonal bovine serum albumin antibodies were studied using force spectroscopy mode of atomic force microscopy. The histograms of the unbinding forces for polyclonal bovine serum albumin antibodies are broad at high antibody concentrations (50 or 270 μg/ml) and narrow at low concentrations (10 or 27 μg/ml), while the histograms for monoclonal antibodies peak at well defined unbinding force. The peak unbinding force depends on the type of antibody and the antibody concentration. In this paper we described and characterized the passive adsorption and covalent immobilization of proteins for tip and sample preparation. Force spectroscopy could serve as a useful method for characterization of antigen-antibody interactions for measuring the specificity of an antibody or to assess the purity of a monoclonal antibody solution and to distinguish between different antibodies.
    Źródło:
    Acta Physica Polonica A; 2003, 104, 3-4; 321-326
    0587-4246
    1898-794X
    Pojawia się w:
    Acta Physica Polonica A
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    AFM Force Spectroscopy and Steered Molecular Dynamics Simulation of Protein Contactin 4
    Autorzy:
    Strzelecki, J.
    Powiązania:
    https://bibliotekanauki.pl/articles/1807636.pdf
    Data publikacji:
    2009-12
    Wydawca:
    Polska Akademia Nauk. Instytut Fizyki PAN
    Tematy:
    82.37.Rs
    87.10.Tf
    Opis:
    We use a single molecule atomic force spectroscopy combined with the steered molecular dynamics simulation to determine a mechanical behavior of neural cell adhesion protein contactin during its unfolding. Force curves typical for modular proteins were observed, showing at most four unfolding peaks. The analysis of force spectra performed within worm-like chain model of polymer elasticity showed the presence of three unfolding lengths. Small plateaus, most likely resulting from forced transitions within domains were observed for the first time. Steered molecular dynamics simulations help to determine atomistic picture of domain unfolding.
    Źródło:
    Acta Physica Polonica A; 2009, 116, S; S-156-S-159
    0587-4246
    1898-794X
    Pojawia się w:
    Acta Physica Polonica A
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Molecular Interaction between Bacterial Antigens and Macrophage Receptors Studied by Atomic Force Microscopy
    Autorzy:
    Targosz, M.
    Czuba, P.
    Biedroń, R.
    Strus, M.
    Gamian, A.
    Marcinkiewicz, J.
    Szymoński, M.
    Powiązania:
    https://bibliotekanauki.pl/articles/2044777.pdf
    Data publikacji:
    2006-03
    Wydawca:
    Polska Akademia Nauk. Instytut Fizyki PAN
    Tematy:
    82.37.Rs
    87.64.Dz
    87.15.Kg
    Opis:
    Atomic force spectroscopy was used to study interaction strengths between bacterial antigens and receptors on macrophages. This method allowed for a direct comparison of the interaction strengths in different systems studied at the level of single molecules.
    Źródło:
    Acta Physica Polonica A; 2006, 109, 3; 421-426
    0587-4246
    1898-794X
    Pojawia się w:
    Acta Physica Polonica A
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Structures in Multicomponent Polymer Films: Their Formation, Observation and Applications in Electronics and Biotechnology
    Autorzy:
    Budkowski, A.
    Bernasik, A.
    Moons, E.
    Lekka, M.
    Zemła, J.
    Jaczewska, J.
    Haberko, J.
    Raczkowska, J.
    Rysz, J.
    Awsiuk, K.
    Powiązania:
    https://bibliotekanauki.pl/articles/1808304.pdf
    Data publikacji:
    2009-02
    Wydawca:
    Polska Akademia Nauk. Instytut Fizyki PAN
    Tematy:
    81.16.Dn
    61.25.H-
    68.37.-d
    82.80.Ms
    85.60.-q
    85.65.+h
    82.37.Rs
    Opis:
    Several strategies to form multicomponent films of functional polymers, with micron, submicron and nanometer structures, intended for plastic electronics and biotechnology are presented. These approaches are based on film deposition from polymer solution onto a rotating substrate (spin-casting), a method implemented already on manufacturing lines. Film structures are determined with compositional (nanometer) depth profiling and (submicron) imaging modes of dynamic secondary ion mass spectrometry, near-field scanning optical microscopy (with submicron resolution) and scanning probe microscopy (revealing nanometer features). Self-organization of spin-cast polymer mixtures is discussed in detail, since it offers a one-step process to deposit and align simultaneously domains, rich in different polymers, forming various device elements: (i) Surface segregation drives self-stratification of nanometer lamellae for solar cells and anisotropic conductors. (ii) Cohesion energy density controls morphological transition from lamellar (optimal for encapsulated transistors) to lateral structures (suggested for light emitting diodes with variable color). (iii) Selective adhesion to substrate microtemplates, patterned chemically, orders lateral structures for plastic circuitries. (iv) Submicron imprints of water droplets (breath figures) decorate selectively micron-sized domains, and can be used in devices with hierarchic structure. In addition, selective protein adsorption to regular polymer micropatterns, formed with soft lithography after spin-casting, suggests applications in protein chip technology. An approach to reduce lateral blend film structures to submicron scale is also presented, based on (annealed) films of multicomponent nanoparticles.
    Źródło:
    Acta Physica Polonica A; 2009, 115, 2; 435-440
    0587-4246
    1898-794X
    Pojawia się w:
    Acta Physica Polonica A
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Titanium Surface Modification with Carbon Nanotubes. Towards Improved Biocompatibility
    Autorzy:
    Benko, A.
    Wiecheć, A.
    Rajchel, B.
    Długoń, E.
    Błażewicz, M.
    Powiązania:
    https://bibliotekanauki.pl/articles/1398806.pdf
    Data publikacji:
    2016-02
    Wydawca:
    Polska Akademia Nauk. Instytut Fizyki PAN
    Tematy:
    68.37.Hk
    78.30.Na
    81.15.Pq
    82.45.Mp
    87.85.J-
    87.85.Rs
    Opis:
    Subject of this study is surface modification of titanium with thin layers of carbon nanotubes, obtained via an electrophoretic deposition, as a means to improve metal's biocompatibility and provide a suitable matrix for very facile further modifications, if needed. Article presents a preliminary evaluation of the material, using goniometer, scanning electron microscopy and the Raman spectroscopy. The layer is found to be composed of randomly distributed, strongly adhered carbon nanotubes, introducing nanotopography to the surface of titanium. Biological studies were conducted with the human osteoblast-like cell line MG63. Biocompatibility of materials was evaluated using: (a) lactate dehydrogenase cytotoxicity test (LDH) and (b) γ -H2AX genotoxicity test (presence of DNA double strand breaks). Results confirmed non-toxic character of the tested materials. Moreover, carbon nanotubes layers enhanced the biocompatibility properties of titanium substrate - material with carbon nanotubes possessed lower cellular toxic properties even than pure titanium. The result of this preliminary study are very promising and may serve as a starting point for further studies, including further chemical or biological modification of the obtained materials.
    Źródło:
    Acta Physica Polonica A; 2016, 129, 2; 176-178
    0587-4246
    1898-794X
    Pojawia się w:
    Acta Physica Polonica A
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
      Wyświetlanie 1-5 z 5

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