3/17/2024 0 Comments Dmpc pro cannot read the game fileThe influence of Ala residue stereochemistry is also reflected in the interactions of the studied peptides with model membranes, as shown by the 31P NMR static spectra, in which the shapes of the phosphorus NMR signals originating from D-isomers correspond to spherically shaped vesicles in the presence of external magnetic field, in comparison to a more elongated ones observed for L-isomers, while TEM photographs shows that upon addition of D-isomers larger lipid vesicles are formed, in contrast to smaller ones for L-isomers. The analysis of ROESY HR MAS spectra of the peptides interacting with the DMPC bilayer indicates that both stereoisomers have still more extended conformation compared to aqueous phase, as shown by much weaker intermolecular interactions. Using two-dimensional NMR techniques we demonstrate that in D 2O/H 2O peptides with D-alanine have extended conformation, while for the L-isomers more compact conformation is preferred. In this work the conformation of dermorphin, Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser-NH 2, an opioid peptide and its analogues with different stereochemistry of alanine and different C-terminus is studied in aqueous and membrane environments.
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