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National Repository of Grey Literature 2 records found  Search took 0.00 seconds. 
Impact of membrane properties on clustering of transmembrane peptides
 Sabó, Ján ; Cebecauer, Marek (advisor) ; Vít, Ondřej (referee)
Unfolded protein response (UPR) is a complex cellular mechanism induced upon ER stress caused by various environmental factors. Single spanning signal transducers of UPR were reported to recognise also lipid-induced ER stress. Studies of these transducers, namely PERK and IRE1 uncovered that they can sense change in membrane properties and activate themselves by clustering. Moreover, signal transducer IRE1 retained ability to sense changes in the membrane properties with TMD exchanged for a polyLeu α-helix. It was thus unclear what mechanism drives lipid-induced UPR via IRE1. We employed model membrane system in form of LUVs, where properties of membranes can be readily altered by specific lipid composition. As a simplified model of the UPR signal transducers in the ER, synthetic transmembrane peptides with polyLeu core were used. Dynamic light scattering (DLS) has been used for qualitative and semi-quantitative analysis of LUVs. Clustering of synthetic peptides was determined by time resolved anisotropy of fluorescence. DLS results demonstrate successful formation of vesicles with a desired size in all planned composition. On the contrary to the studies in living cells, the presence of cholesterol or palmitic acid in model membranes did not induce the aggregation of transmembrane peptides....
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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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