A variety of amphiphilic helical peptides have been shown to exhibit a transition from
adsorbing parallel to a membrane surface at low concentrations to inserting perpendicularly …

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 …

Samples of pure lipid (dipalmitoylphosphatidylcholine) and lipid containing short α-helical
peptides were oriented and examined by X-ray diffraction, together with unoriented samples …

Adsorption of amphiphilic peptides to the headgroup region of a lipid bilayer is a common
mode of protein-membrane interactions. Previous studies have shown that adsorption …

The amphipathic helix, in which hydrophobia and hydrophilic residues are grouped on
opposing faces, is a structural mot if found in many peptides and proteins that bind to …

Amphiphilic helical peptides exhibit an insertion transition when they interact with lipid
bilayers. At low concentrations, the peptides adsorb at the hydrophilic-hydrophobic interface …

Alamethicin adsorbs on the membrane surface at low peptide concentrations. However,
above a critical peptide-to-lipid ratio (P/L), a fraction of the peptide molecules insert in the …

Model compounds of modified hydrophobicity (H), hydrophobic moment (μ) and angle
subtended by charged residues (Φ) were synthesized to define the general roles of …

James H. Davis,* Donna M. Clare, Robert S. Hodges, and Myer Bloom abstract: A unique
model-membrane system composed of synthetic amphiphilic peptides, as models of …

We have investigated the effect of several hydrophobic polypeptides on the phase behavior
of diacylphosphatidylcholines with different acyl chain length. The polypeptides are …