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- W2014454732 abstract "Abstract Tridecaptin A 1 is a linear antimicrobial lipopeptide comprised of 13 amino acids, including three diaminobutyric acid (Dab) residues. It displays potent activity against Gram‐negative bacteria, including multidrug‐resistant strains. Using solid‐phase peptide synthesis, we performed an alanine scan of a fully active analogue, octyl‐tridecaptin A 1 , to determine key residues responsible for activity. The synthetic analogues were tested against ten organisms, both Gram‐positive and Gram‐negative bacteria. Modification of D ‐Dab8 abolished activity, and marked decreases were observed with substitution of D ‐allo‐Ile12 and D ‐Trp5. Circular dichroism showed that octyl‐tridecaptin A 1 adopts a secondary structure in the presence of model phospholipid membranes, which was weakened by D ‐Dab8‐ D ‐Ala, D ‐allo‐Ile12‐ D ‐Ala, and D ‐Trp5‐ D ‐Ala substitutions. The antimicrobial activity of the analogues is directly correlated to their ability to adopt a stable secondary structure in a membrane environment." @default.
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- W2014454732 date "2014-05-09" @default.
- W2014454732 modified "2023-10-12" @default.
- W2014454732 title "Key Residues in Octyl-Tridecaptin A<sub>1</sub>Analogues Linked to Stable Secondary Structures in the Membrane" @default.
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- W2014454732 doi "https://doi.org/10.1002/cbic.201402024" @default.
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