{"id":{"repo_id":"aachen","oai_identifier":"oai:publications.rwth-aachen.de:61971"},"canonical_url":"https://search.dev.ndltd.org/etd/aachen/oai:publications.rwth-aachen.de:61971","repository":{"repo_id":"aachen","name":"RWTH Aachen University","base_url":"https://publications.rwth-aachen.de/oai2d"},"display":{"title":"Effect of 2,4-dichlorophenol on biological model membranes","abstract":"The aim of this work was to examine molecular factors and processes with respect to the uptake, distribution and effects of chlorophenol derivatives inside the cell membrane of microorganisms, particularly in the phospholipid bilayer matrix. 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) multilamellar vesicles as a model membrane were used to study the behavior of cell membranes in the presence of 2,4-dichlorophenol (DCP) using following methodes: differential scanning calorimetry (DSC), small- (SAXS) and wide-angle X-ray scattering (WAXS), freeze-fracture/TEM and FT-Raman spectroscopy. The results suggested that the effect of DCP on the liposomes properties was highly concentration-dependent. The presence of DCP molecules at low concentrations induced a more symmetrical structure of lipid bilayers reducing the structural defects. Its perturbing effect appeared first if the DCP concentration was higher than the structural defects in the lipid layers lattices and became drastical above the DCP/lipid ratio of 1/2. By these molar ratios the fluid-crystalline phase became dominant inducing a highly fluid membrane structure also in the gel phase temperature region. The inhomogeneous distribution of DCP caused a lateral separation of lipid domains. It is hypothesized that the uptake of DCP by lipid bilyers is limited and a part of DCP molecules form clusters which horizontally separat the lipid-layer domains destroying the closed bilayer sheets. The phospholipid-membrane features changed may influence the transport processes and lipid-protein interactions in the biological membranes.","abstract_html":"The aim of this work was to examine molecular factors and processes with respect to the uptake, distribution and effects of chlorophenol derivatives inside the cell membrane of microorganisms, particularly in the phospholipid bilayer matrix. 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) multilamellar vesicles as a model membrane were used to study the behavior of cell membranes in the presence of 2,4-dichlorophenol (DCP) using following methodes: differential scanning calorimetry (DSC), small- (SAXS) and wide-angle X-ray scattering (WAXS), freeze-fracture/TEM and FT-Raman spectroscopy. The results suggested that the effect of DCP on the liposomes properties was highly concentration-dependent. The presence of DCP molecules at low concentrations induced a more symmetrical structure of lipid bilayers reducing the structural defects. Its perturbing effect appeared first if the DCP concentration was higher than the structural defects in the lipid layers lattices and became drastical above the DCP/lipid ratio of 1/2. By these molar ratios the fluid-crystalline phase became dominant inducing a highly fluid membrane structure also in the gel phase temperature region. The inhomogeneous distribution of DCP caused a lateral separation of lipid domains. It is hypothesized that the uptake of DCP by lipid bilyers is limited and a part of DCP molecules form clusters which horizontally separat the lipid-layer domains destroying the closed bilayer sheets. 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The results suggested that the effect of DCP on the liposomes properties was highly concentration-dependent. The presence of DCP molecules at low concentrations induced a more symmetrical structure of lipid bilayers reducing the structural defects. Its perturbing effect appeared first if the DCP concentration was higher than the structural defects in the lipid layers lattices and became drastical above the DCP/lipid ratio of 1/2. By these molar ratios the fluid-crystalline phase became dominant inducing a highly fluid membrane structure also in the gel phase temperature region. The inhomogeneous distribution of DCP caused a lateral separation of lipid domains. It is hypothesized that the uptake of DCP by lipid bilyers is limited and a part of DCP molecules form clusters which horizontally separat the lipid-layer domains destroying the closed bilayer sheets. 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