Intraocular liquid, in contrast to blood, has no cellular components; therefore, proteins (human serum albumin [HSA], and [alpha, beta, gamma] globulins) are the major components that determine patients' response to the intraocular lens (IOL) surface. In addition to the amount of adsorbed proteins, the possibility of its conformational changes, including conformational changes of globulins C1 and C3 that respond for the activation of the complements system by the classical and alternative pathways, cannot be excluded. The interaction between IOLs and protein components of intraocular liquid directly influences the ocular exudative reaction in the early postoperational period, the intensity of cellular and pigmental scurf on the surface of the IOLs, and the state of endothelial cells of the cornea in the distant postoperational period. Our goal was to compare the interaction of commercial IOLs made from polymethylmethacrylate, silicone, poly-2-hydroxyethyl methacrylate (p-HEMA), and copolymer p-HEMA with collagen with HSA and the complement system. The total internal reflection fluorescence (TIRF) method and hemolytic assay were used for this task, respectively. It has been demonstrated that the probability of biocompatibility of commercially produced IOLs on the stage of protein adsorption can be evaluated using the kinetic of HSA-fluorescein isothiocyanate adsorption onto the IOL surface by the TIRF METHOD: In the case of IOLs from p-HEMA, a negative correlation was shown between the degree of irreversible adsorption of HSA and the minimum relative rate constant of the surface-induced complement activation. We did not find any correlation between hydrophilicity/hydrophobicity of lenses and their adsorptional properties including complement activation. From suggested adsorptional criteria in vitro for biocompatible surfaces, the hydrogel lens from p-HEMA has a lower probability of biocompatibility in comparison with other IOLs.
One of the most important applications of polymeric porous nanomaterials is the design of nanoporous structures for operation in patch-clamp systems allowing to establish a gigaohm contact, as well as for the measurements of biomolecules, informational macromolecules, including DNA, translocating through the nanopore arrays. Development of nanopore sequencing techniques leads to fundamentally new big data arrays, but their representativeness and validity, as well as the validity of counting of biomacromolecular particles based on ultramicropore arrays, strongly depends both on the pore size (in engineering lithography unimodal pore size distribution is optimal) and the accuracy of the size distribution measurements using instrumental methods. However, the former is unattainable when using soft matter or stretchable, plastic and elastic polymer materials and films, while the latter depends on the metrological parameters of the instrumental and algorithmic porosimetry techniques. Therefore in this paper the question about the applicability of polymer materials with pore arrays for the studies of biomacromolecules and bionanostructures is proposed to be answered using a comparative analysis of two different porosimetry approaches with the resolution not lower than electron microscopic one.
~u~onAdsorption of proteins is the primary reaction of blood and other biological fluids brought into contact with medical materials or devices. This explains the considerable interest in mechanisms of biological compatibility of foreign surfaces at the 9 stage of protein adsorption and in the search for adsorption criteria of biocompatibility of medical materials or devices /n vitro [2]. The interaction of proteins with various surfaces of medical devices (films, plates, tubes, etc.) is presently extensively studied by various physical and chemical methods (radionuclides, infrared spectroscopy, fluorescence spectroscopy, ellipsometry, atomic force microscopy, etc.). However, biocompatibility of a given device depends not only on chemical structure of its materials, but also on its design and manufacturing technology. In addition, functional conditions (duration of exposure to biological tissues, place of location, composition of surrounding medium, etc.) also affect the biocompatibility of the device [3].The type of protein adsorption plays a very important role in biocompatibility and functional properties of intraocular lenses (IOL) made of polymethylmetacrylate (PMMA), polyorganosiloxanes (silicon), and polyhydroxyethylmetacrylate (p-HEMA) [5]. In contrast to blood, intraocular fluid is virtually free of ceils. Therefore, proteins (albumin, a-globulin, E-globulin, and 7-globulin) are major components of the biological medium that determine a patient's reaction to implanted IOL. In addition to the amount of adsorbed protein, the possibility of conformational changes of proteins (including immunoglobulins C1 and (23) should also be taken into consideration. This is of particular importance because immunoglobulins C1 and C3 are responsible for activation of the complement system by the classical and alternative mechanisms, respectively [2, 51. Interaction between implant and protein components of intraocular fluid has a substantial effect on the exudative reaction of the eye during the early postoperative period, the intensity of cellular and pigment deposition on the IOL surface, and the state of corneal endothelial cells during the remote postoperative period.It was shown in [1, 4] that the fluorescence method of total internal reflection (FTIR) can be used for studying the kinetics of adsorption of blood plasma proteins (albumin, 7-globulin, fibrinogen) from solution to the surface of polymer and quartz films.The goal of this work was to use the FFIR method for studying adsorption and desorption of proteins at the IOL surface. Materials and MethodsFour types of IOL manufactured at the Scientific Experimental Works Eye Microsurgery, Ltd. were used: -serially produced IOL made of PMMA; -laboratory prototype IOL samples made of silicon composite material SIEL-Med with additionally treated surface; -laboratory prototype hydrogel IOL samples made of p-HEM.A;
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