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    Wyświetlanie 1-4 z 4
    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:
    AFM Investigation of Biological Nanostructures
    Autorzy:
    Strzelecki, J.
    Dąbrowski, M.
    Strzelecka, J.
    Tszydel, M.
    Mikulska, K.
    Nowak, W.
    Balter, A.
    Powiązania:
    https://bibliotekanauki.pl/articles/1419535.pdf
    Data publikacji:
    2012-08
    Wydawca:
    Polska Akademia Nauk. Instytut Fizyki PAN
    Tematy:
    87.64.Dz
    81.07.-b
    Opis:
    Nanostructures created by living organisms, optimized through millions of years of evolution, can be a valuable inspiration for nanotechnology. We employ atomic force microscopy to examine such structures in materials created by common organisms - caddisfly and diatoms. Caddisfly larvae are well known for their ability to spin silk, which serves as an "adhesive tape" to glue various materials and collect food in aqueous environment. Atomic force microscopy imaging of caddisfly silk, performed for the first time by our team, has shown that its surface is patterned with 150 nm extensions - a feature related to its exceptional underwater sticking abilities. Results of force spectroscopy of protein structures found on the surface are also shown. A characteristic feature of diatoms is that they are encased within a unique silica cell wall called frustules, patterned with 200 nm pores, which allow cellular interaction with the environment. We perform atomic force microscopy imaging of frustules in living diatoms as well as adhesion measurements inside pores.
    Źródło:
    Acta Physica Polonica A; 2012, 122, 2; 329-332
    0587-4246
    1898-794X
    Pojawia się w:
    Acta Physica Polonica A
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Study of Adhesion Interaction Using Atomic Force Microscopy
    Autorzy:
    Gryboś, J.
    Pyka-Fościak, G.
    Lebed, K.
    Lekka, M.
    Stachura, Z.
    Styczeń, J.
    Powiązania:
    https://bibliotekanauki.pl/articles/2038080.pdf
    Data publikacji:
    2004-05
    Wydawca:
    Polska Akademia Nauk. Instytut Fizyki PAN
    Tematy:
    87.64.Dz
    68.35.Gy
    Opis:
    An atomic force microscope is a useful tool to study the interaction forces at molecular level. In particular the atomic force microscope can measure an unbinding force needed to separate the two single molecule complexes. Recent studies have shown that such unbinding force depends linearly on the logarithm of the applied loading rate, defined as a product of scanning velocity and the spring constant characterizing the investigated system (cantilever vs. surface). This dependence can be used to study the energy landscape shape of a molecular complex by the estimation of energy barrier locations and the related dissociation rates. In the present work the complex consisting of ethylene(di)aminetetraacetic acid and the bovine serum albumin was measured. The dependence between the unbinding force and the logarithm of the loading rate was linear. Using the Bell model describing the dissociation of the above molecules caused by the action of the external bond breaking force, two parameters were estimated: the dissociation rate and the position of the energy barrier needed to overcome during a transition from a bound to unbound state. The obtained results are similar to those obtained for a typical ligand-receptor interaction.
    Źródło:
    Acta Physica Polonica A; 2004, 105, 5; 501-510
    0587-4246
    1898-794X
    Pojawia się w:
    Acta Physica Polonica A
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Atomic Force Microscopy and Quartz Crystal Microbalance Study of the Lectin-Carbohydrate Interaction Kinetics
    Autorzy:
    Lebed, K.
    Kulik, A. J.
    Forró, L.
    Lekka, M.
    Powiązania:
    https://bibliotekanauki.pl/articles/2047270.pdf
    Data publikacji:
    2007-02
    Wydawca:
    Polska Akademia Nauk. Instytut Fizyki PAN
    Tematy:
    87.64.Dz
    84.37.+q
    87.15.Kg
    82.37.Np
    81.65.Cf
    52.77.Bn
    Opis:
    Two analytical methods, atomic force microscopy and quartz crystal microbalance, were applied to the study of the reaction kinetics occurring between concanavalin A and carboxypeptidase Y, presenting the specific lectin-carbohydrate recognition. The dissociation rate constants for concanavalin A-carboxypeptidase Y complex obtained using both atomic force microscopy and quartz crystal microbalance were of the same order of magnitude: k$\text{}_{diss}$=0.170± 0.060 s$\text{}^{-1}$ and k$\text{}_{diss}$=0.095±0.002 s$\text{}^{-1}$, respectively. In addition, each method alone aided in determining other parameters characterizing the studied interaction. Quartz crystal microbalance permitted us to estimate the association rate (k$\text{}_{ass}$=(5.6 ±0.1)×10$\text{}^{4}$ M$\text{}^{-1}$ s$\text{}^{-1}$) and the equilibrium (K$\text{}_{a}$=(0.59×0.01)×10$\text{}^{6}$ M$\text{}^{-1}$) constants for the binding process occurring between concanavalin A and mannose residues of carboxypeptidase Y under given experimental conditions. Atomic force microscopy in force spectroscopy mode enabled the determination of the energy barrier position of r=2.29±0.04 Å characterizing the dissociation of concanavalin A- carboxypeptidase Y molecular complex. The presented results show that both atomic force microscopy and quartz crystal microbalance can be used to determine quantitative parameters characterizing the specific molecular interaction. Both methods can be easily combined for complementary and/or alternative studies of a chosen molecular interaction. By preparing the samples in the same manner the direct comparison between the data obtained via atomic force microscopy and quartz crystal microbalance can be made.
    Źródło:
    Acta Physica Polonica A; 2007, 111, 2; 273-286
    0587-4246
    1898-794X
    Pojawia się w:
    Acta Physica Polonica A
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
      Wyświetlanie 1-4 z 4

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