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A new method for double bond characterization in lipids by ultraviolet photodissociation mass spectrometry
Rumlová, Barbora ; Strmeň, T. ; Cvačka, Josef
Lipids are structurally diverse biomolecules with vital functions in biological systems. Some of these functions are closely associated with the specific location of the carbon-carbon double bond in the lipid acyl chains. The chain length and the number of unsaturated carbon-carbon bonds can be determined using conventional MS/MS-based structural elucidation methods employing low or higher energy collision-induced dissociation. However, these dissociation techniques do not provide more subtle structural details, for example, the position of unsaturated bonds. Another type of activation method – ultraviolet photodissociation can be used for this purpose. In this study, a new method for characterization of double bond location in lipids acyl chain was developed using 193 nm ultraviolet photodissociation implemented on Orbitrap Fusion Lumos mass spectrometer. This approach is based on the derivatization of the double bond with bis-(5-iodo-[2]pyridyl)-disulfide, subsequent specific cleavages provide a unique diagnostic pair bearing information about the double bond position.
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Quantum dot luminescent probe for Caspase 3/7 imaging inside cells
Procházková, Markéta ; Klepárník, Karel
Two step synthesis of luminescent probe based on ligand-exchange in the first step and the specific reaction of amino group in the second step was optimized. The luminescence properties of the final product were checked by time course of\nactive recombinant caspase protein reaction under the model conditions in fluorimeter. The novel luminescent probe enables long-time imaging of active caspases in living cells or tissues.
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Epitachophoretic preconcentration of proteins
Hrušková, Helena ; Voráčová, Ivona ; Foret, František
In this work, we present a developed method for preconcentration of standards of proteins cytochrome c, myoglobin, and hemoglobin. Firstly, the electrolyte system was selected and optimized to provide low analysis time, narrow shape of the protein zone, and eliminate overheating at the center of the device. In the next step, the developed method was tested on the preconcentration of proteins: cytochrome c, myoglobin, and hemoglobin. After several adjustments myoglobin and hemoglobin were also uccessfully preconcentrated. After evaluation of pilot results, this technique provides up to fiftyfold preconcentration and recovery of over 70 % for each protein. The next plan is to preconcentrate proteins from complex biological matrices such as urine or blood plasma.
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