Conspectus The structures of membrane-bound polypeptides are intimately related to their
functions and may change dramatically with the lipid environment. Circular dichroism (CD) is …

Solid-state NMR spectroscopic techniques provide valuable information about the structure,
dynamics and topology of membrane-inserted polypeptides. In particular antimicrobial …

Hydrophobic mismatch is important for pore-forming amphipathic antimicrobial peptides, as
demonstrated recently [Grau-Campistany, A., et al.(2015) Sci. Rep. 5, 9388]. A series of …

The membrane alignment of the amphiphilic α-helical model peptide MSI-103 (sequence
[KIAGKIA] 3-NH2) was examined by solid state 2H-NMR in different lipid systems by …

The interaction of membranes with peptides and proteins is largely determined by their
amphiphilic character. Hydrophobic moments of helical segments are commonly derived …

Gram-negative bacteria are becoming resistant to almost all currently available antibiotics.
Systemically designed antimicrobial peptides (AMPs) are attractive agents to enhance the …

BP100 is a multifunctional membrane-active peptide of only 11 amino acids, with a high
antimicrobial activity, an efficient cell-penetrating ability, and low hemolytic side-effects. It …

The folding and function of membrane proteins is controlled not only by specific but also by
unspecific interactions with the constituent lipids. In this review, we focus on the influence of …

Plasticins (PTC) are dermaseptin-related antimicrobial peptides characterized by a large
number of leucine and glycine residues arranged in GXXXG motifs that are often described …

Amphipathic peptides can act as antibiotics due to membrane permeabilization. KL peptides
with the repetitive sequence [Lys-Leu] n-NH2 form amphipathic β-strands in the presence of …