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Mass spectrometry analysis of integral membrane peptides
 Sabó, Ján ; Cebecauer, Marek (advisor) ; Pompach, Petr (referee)
Biological membranes ensure a large scale of vital processes in the living organisms. Lipid and protein composition is very complex in the membranes. Therefore, simplified model systems were developed to study basic mechanisms regulating the function of membranes. To simulate transmembrane proteins of the type I and II, the short, α-helix-forming, synthetic peptides are employed. The hydrophobic character of the peptides and their transbilayer positioning in membranes well represents transmembrane domains of proteins in the living organisms. One of the simplest and most widely used model membrane systems are liposomes. Methods for their formation has been known for a long time. Quantification of their components after the process of liposome preparation is challenging, but for the maximal control over given model system very desirable. In this work, we adapted a formerly described protocol for delipidisation of the transmembrane peptides for their consequent characterisation by LC/MS. A relative amount of peptide successfully incorporated into vesicles was acquired by the analysis of extracted chromatograms of peptide ions. We demonstrate that analysis of vesicles with peptide content of 5-10 mol% is feasible and the loss of the peptide is below 50 %. Such vesicles can be used for further...
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