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Force Spectroscopy of Polyclonal and Monoclonal Anti-Bovine Serum Albumin Antibodies - BSA Complexes

100%
Chtcheglova L., Dietler G.
Acta Physica Polonica A
|
2003
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vol. 104
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issue 3-4
321-326
EN
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.
2
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AFM Force Spectroscopy and Steered Molecular Dynamics Simulation of Protein Contactin 4

100%
Strzelecki J.
Acta Physica Polonica A
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2009
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vol. 116
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issue S
S-156-S-159
EN
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.
3
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Molecular Interaction between Bacterial Antigens and Macrophage Receptors Studied by Atomic Force Microscopy

80%
Targosz M., Czuba P., Biedroń R., Strus M., Gamian A., Marcinkiewicz J., Szymoński M.
Acta Physica Polonica A
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2006
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vol. 109
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issue 3
421-426
EN
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.
4
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Structures in Multicomponent Polymer Films: Their Formation, Observation and Applications in Electronics and Biotechnology

61%
Budkowski A., Bernasik A., Moons E., Lekka M., Zemła J., Jaczewska J., Haberko J., Raczkowska J., Rysz J., Awsiuk K.
Acta Physica Polonica A
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2009
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vol. 115
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issue 2
435-440
EN
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.
5
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Biophysical changes induced by cholesterol on phosphatidylcholine artificial biomembranes containing alamethicin oligomers

51%
Cernescu A., Luchian T.
Open Physics
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2006
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vol. 4
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issue 2
155-167
EN
Cholesterol is an important constituent of eukaryotic cell membranes, whose interaction with phospholipids leads to a broad range of biological roles, such as: maintenance of proper fluidity, formation of raft domains, reduction of passive permeability of various chemical species through the bilayer (e.g., glucose, glycerol, K+, Na+ and Cl− ions), and increased mechanical strength of the membrane. In this work we studied an interesting paradigm, as to whether cholesterol-containing phosphatidylcholine biomembranes influence the kinetics and transport features of alamethicin oligomers embedded into it. We demonstrate that moderate relative amounts of cholesterol increase the electrical conductance of various sub-conductance states of the alamethicin oligomer, caused probably by a non-monotonic change in the lumped dipole moment of the biomembrane. Our data suggest that biomembrane stiffness caused by cholesterol, visibly modifies the association-dissociation rates of alamethicin oligomerization in the biomembrane. Moreover, increasing concentrations of cholesterol seem to lead to more stable intermediate alamethicin oligomers. We show that in the presence of cholesterol, as the diameter of the alamethicin oligomer increases, so does the time of another monomer to get picked up. These results brings into focus the interesting issue of how oligomerization of proteins affects their interaction affinities for membrane-based lipids.
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