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Using 2-D electrophoresis followed by nano HPLC in nuclear protein analysis of MCF-7 breast cancer cell line by MALDI-TOF/TOF

100%

Tkáčiková S., Talian I., Petrovič M., Sabo J.

Open Chemistry

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2012

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vol. 10

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issue 2

407-412

EN

The biomarker identification is an important tool in early cancer detection. The MCF-7 breast cancer cell line was chosen as a model system. The nuclear proteins were extracted utilizing a commercially manufactured kit and separated on two dimensional (2-D) sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS PAGE). The first dimension was performed on isoelectric focusing strips with pH range 4–7. Afterwards the proteins were tryptic digested and identification was performed by matrix assisted laser desorption technique with time of flight mass analyzer (MALDI-TOF/TOF). For unambiguous identification proteins with too low concentration or spots contains protein mixture the nano high performance liquid chromatography (HPLC) was used. The 2-D gel electrophoresis (2-DGE) seems to be a good tool to separate large amount of proteins using relatively simple procedure and its hyphenation with HPLC can create the perfect analytical solution for proteome identification. About 150 nuclei protein spots were visualized and the most abundant of them were identified. [...]

2

Impact of un-polymerized acrylamide monomer residues onto protein identification by MALDI TOF MS

100%

Talian I., Kováčová V., Petrovič M., Sabo J.

Open Chemistry

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2012

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vol. 10

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issue 4

1073-1078

EN

Polyacrylamide gel electrophoresis is a powerful tool for protein mixture separation frequently used in proteomic studies. This article describes the problems which can arise during the identification process of separated proteins by matrix assisted laser desorption/ionization mass spectrometry. Presence of residual acrylamide monomers in the peptide samples leads to a significant peptide signal suppression. In the case of protein prohibitin, isolated from the MCF 7 breast cancer cell line, the peptide signal suppression was observed in 50% of all detected peptides. [...]

3

TOF-SIMS surface analysis of L-Tryptophan self assembled monolayer

88%

Petrovic M., Talian I., Skantarova L., Orinak A., Velic D.

Open Chemistry

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2014

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vol. 12

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issue 5

568-576

EN

This paper dealt with the preparation and characterization of self - assembled monolayersSAM-s of 1-hexadecanethiole and mercapto acetic acid on the silver nanostructure and subsequently the immobilization with amino acid L-Tryptophane. In order to achieve it, we used the electrodeposition of silver onto nanostructured surface of paraffin impregnated graphite electrode (PIGE). Subsequently, we assembled SAM by choosing the 1-hexadecanethiole and mercaptoacetic acid. These two kinds of SAM underwent the functionalization by L-Tryptophan. The observations of silver on PIGE surfaces were performed by scanning electron microscope (SEM). For surface analysis of the SAM functionalized by L-tryphophan, the TOF-SIMS technique was chosen. Finally, the fragmented ions of the immobilized-L-Tryptophan SAM were determined on the basis of suggested residues and three-dimensional structure. The residues show that the ability of L-Tryptophan to build homogeneous structure is better by mercaptoacetic acid SAM structure than by 1-hexadecanethiol. It was observed that L-Tryptophan built compact surface, which, due its chemical properties, can represent very interesting side regarding biocompatibility, homochirality and robustness in the area of life science.

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3 Open Chemistry

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3 Talian I.

2 Petrovič M.

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1 Orinak A.

1 Petrovic M.

1 Skantarova L.

1 Tkáčiková S.

1 Velic D.

Using 2-D electrophoresis followed by nano HPLC in nuclear protein analysis of MCF-7 breast cancer cell line by MALDI-TOF/TOF

Impact of un-polymerized acrylamide monomer residues onto protein identification by MALDI TOF MS

TOF-SIMS surface analysis of L-Tryptophan self assembled monolayer