Lipoproteins are responsible for cholesterol traffic in humans. Low density lipoprotein (LDL) delivers cholesterol from liver to peripheral tissues. A misleading delivery can lead to the formation of atherosclerotic plaques. LDL has a single protein, apoB-100, that binds to a specific receptor. It is known that the failure associated with a deficient protein-receptor binding leads to plaque formation. ApoB-100 is a large single lipid-associated polypeptide difficulting the study of its structure. IR spectroscopy is a technique suitable to follow the different conformational changes produced in apoB-100 because it is not affected by the size of the protein or the turbidity of the sample. We have analyzed LDL spectra of different individuals and shown that, even if there are not big structural changes, a different pattern in the intensity of the band located around 1617 cm−1 related with strands embedded in the lipid monolayer, can be associated with a different conformational rearrangement that could affect to a protein interacting region with the receptor.
In table olives showing the green staining alteration, extracts of pigment-lipoprotein complexes were obtained from the zone altered and the rest of the fruit. In the altered zone of the olive, the surrounding components of pigments were affected, with the degeneration of proteins and phospholipids forming the pigment-lipoprotein complexes. There was also less interaction between the pigments and the membrane lipids. These results suggested a greater loss of cell integrity in the green-stained zone of the fruit, allowing the migration and local accumulation of Cu-metallochlorophyll complexes, macroscopically visible as the form of green staining alteration.
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