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Báo cáo khoa học: Structures and mode of membrane interaction of a short a helical lytic peptide and its diastereomer determined by NMR, FTIR, and fluorescence spectroscopy
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The interactionofmany lytic cationic antimicrobial peptides with their target cells involves electrostatic interactions, hydrophobic effects, and the formation of amphipathic sec-ondary structures, such asahelices orbsheets. We have shown in previous studies that incorporating 30% D-aminoacids intoashortahelical lyticpeptidecomposedof leucine and lysine preserved the antimicrobial activity of the parent peptide, while the hemolytic activity was abolished.
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