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Study of possibilities of increasing the biocompatibility of organic semiconductor surfaces
Malečková, Romana ; Šafaříková, Eva (referee) ; Vala, Martin (advisor)
This bachelor thesis deals with the possibility of biocompatibilization of organic semiconducting polymer PEDOT:PSS using RGD peptide for the construction of biosensors. Samples were prepared and compared where the RGD peptide was bound directly, as well as samples with a peptide bound via crosslinker molecule sulfo-SANPAH. Whether the RGD peptide was bound to the substrate was determined by the method of measuring the contact angle of liquids with subsequent calculation of surface energy. The results were further verified by elemental analysis, infrared spectrometry and Raman spectroscopy.
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Specific prion protein antibodies characterisation and use in diagnostic
Šafaříková, Eva ; Holada, Karel (advisor) ; Mareš, Michael (referee) ; Živný, Jan (referee)
Transmissive spongiform encephalopathies (TSEs) are neurodegenerative diseases characterized by depositions of abnormally folded prion protein (PrPTSE ) in brain. PrPTSE is at present the only specific biochemical marker of human and animal TSEs. Diagnostic tests are based on the detection of PrPres after proteinase K digestion of brain homogenate using Western blot or on the immunohistochemistry of fixed brain tissue, which are both difficult and time consuming. In this work we focused on development of a new type of tests based on PrP detection without need of proteinase K digestion. As deposits of PrPTSE remain in the body for a long time, there is a substantial chance of them being nonenzymatically modified by glycation. The detection of glycated PrPTSE may have a potential to serve as a diagnostic marker. We prepared monoclonal antibodies specific for carboxymethyl lysine/arginine modified prion protein. Bacterially expressed and purified recombinant human prion protein (rhPrP) was modified by glyoxylic acid that introduces carboxymethyl groups on lysine and arginine residues present within the molecule of the protein. Modified rhPrP (rhPrP-CML) was used for immunization of laboratory mice and hybridoma cells were prepared. Screening of cell supernatants resulted in the selection of 4...
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Study of possibilities of increasing the biocompatibility of organic semiconductor surfaces
Malečková, Romana ; Šafaříková, Eva (referee) ; Vala, Martin (advisor)
This bachelor thesis deals with the possibility of biocompatibilization of organic semiconducting polymer PEDOT:PSS using RGD peptide for the construction of biosensors. Samples were prepared and compared where the RGD peptide was bound directly, as well as samples with a peptide bound via crosslinker molecule sulfo-SANPAH. Whether the RGD peptide was bound to the substrate was determined by the method of measuring the contact angle of liquids with subsequent calculation of surface energy. The results were further verified by elemental analysis, infrared spectrometry and Raman spectroscopy.
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Specific prion protein antibodies characterisation and use in diagnostic
Šafaříková, Eva ; Holada, Karel (advisor) ; Mareš, Michael (referee) ; Živný, Jan (referee)
Transmissive spongiform encephalopathies (TSEs) are neurodegenerative diseases characterized by depositions of abnormally folded prion protein (PrPTSE ) in brain. PrPTSE is at present the only specific biochemical marker of human and animal TSEs. Diagnostic tests are based on the detection of PrPres after proteinase K digestion of brain homogenate using Western blot or on the immunohistochemistry of fixed brain tissue, which are both difficult and time consuming. In this work we focused on development of a new type of tests based on PrP detection without need of proteinase K digestion. As deposits of PrPTSE remain in the body for a long time, there is a substantial chance of them being nonenzymatically modified by glycation. The detection of glycated PrPTSE may have a potential to serve as a diagnostic marker. We prepared monoclonal antibodies specific for carboxymethyl lysine/arginine modified prion protein. Bacterially expressed and purified recombinant human prion protein (rhPrP) was modified by glyoxylic acid that introduces carboxymethyl groups on lysine and arginine residues present within the molecule of the protein. Modified rhPrP (rhPrP-CML) was used for immunization of laboratory mice and hybridoma cells were prepared. Screening of cell supernatants resulted in the selection of 4...
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