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• W4319318525 startingPage "196" @default.
• W4319318525 abstract "Peptides play a critical role in the life of organisms, performing completely different functions. The biological activity of some peptides, such as cyclosporins, can be determined by the degree of membrane permeability. Thus, it becomes important to study how the molecule interacts with lipid bilayers. Cyclosporins C, E, H and L were characterised molecular dynamics simulation; NMR spectroscopy studies were also carried out for cyclosporins C and E. The comparison of one- and two-dimensional spectra revealed certain similarities between spatial structures of the studied cyclosporin variants. Upon dissolving in water containing DPC micelles, which serve as model membranes, subtle changes in the NMR spectra appear, but in a different way for different cyclosporins. In order to understand whether observed changes are related to any structural modifications, simulation of the interaction of the peptide with the phospholipid micelle was performed. The onset of the interaction was observed, when the peptide is trapped to the surface of the micelle. Simulations of this kind are also of interest in the light of the well-known membrane permeability of cyclosporin, which is important for its biological action." @default.
• W4319318525 created "2023-02-08" @default.
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• W4319318525 date "2023-02-05" @default.
• W4319318525 modified "2023-09-30" @default.
• W4319318525 title "Binding of Different Cyclosporin Variants to Micelles Evidenced by NMR and MD Simulations" @default.
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• W4319318525 doi "https://doi.org/10.3390/membranes13020196" @default.
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• W4319318525 hasPublicationYear "2023" @default.
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