## Abstract In our previous study, we utilized a 26‐residue amphipathic α‐helical antimicrobial peptide L‐V13K (Chen et al., Antimicrob Agents Chemother 2007, 51, 1398–1406) as the framework to study the effects of peptide hydrophobicity on the mechanism of its antimicrobial action. In this study,
Stabilizing effects of 2-methylalanine residues on β-turns and α-helices
✍ Scribed by G. Jung; R. Bosch; E. Katz; H. Schmitt; K.-P. Voges; W. Winter
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1983
- Tongue
- English
- Weight
- 255 KB
- Volume
- 22
- Category
- Article
- ISSN
- 0006-3525
No coin nor oath required. For personal study only.
✦ Synopsis
An N-terminal rigid a-helical segment is found in the polypeptide antibiotics alamethicin, suzukacillin, and trichotoxin. The a-helix dipole is essential for their voltage-dependent pore formation in lipid bilayer membranes, which is explained by a flip-flop gating mechanism based on dipole-dipole interactions of parallel and antiparallel arranged a-helices within oligomeric structures.
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