AbstractAntimicrobial peptides have two binding states in a lipid bilayer, a surface state S and a pore-forming state I. The transition from the S state to the I state has a sigmoidal peptide-concentration dependence indicating cooperativity in the peptide-membrane interactions. In a previous paper, we reported the transition of alamethicin measured in three bilayer conditions. The data were explained by a free energy that took into account the membrane thinning effect induced by the peptides. In this paper, the full implications of the free energy were tested by including another type of peptide, melittin, that forms toroidal pores, instead of barrel-stave pores as in the case of alamethicin. The S-to-I transitions were measured by oriente...
AbstractWe present an experimental study of the pore formation processes of small amphipathic peptid...
AbstractThe transition of the state of alamethicin from its inactive state to its active state of po...
We present an experimental study of the pore formation processes of small amphipathic peptides in mo...
ABSTRACT: Antimicrobial peptides are known to form pores in cell membranes. We study this process in...
AbstractRecently we have shown that the free energy for pore formation induced by antimicrobial pept...
AbstractRecently we have shown that the free energy for pore formation induced by antimicrobial pept...
The mechanism of pore formation of lytic peptides, such as melittin from bee venom, is thought to in...
Alamethicin is a transmembrane ion channel at low concentration, and a lytic agent of cell membrane ...
The mechanism of pore formation of lytic peptides, such as melittin from bee venom, is thought to in...
Adsorption of amphiphilic peptides to the headgroup region of a lipid bilayer is a common mode of pr...
Alamethicin adsorbs on the membrane surface at low peptide concentrations. However, above a critical...
Alamethicin adsorbs on the membrane surface at low peptide concentrations. However, above a critical...
Using dilatometry and small-angle X-ray diffraction, we have studied under bulk conditions the struc...
The mechanism of pore formation of lytic peptides, such as melittin from bee venom, is thought to in...
AbstractBased on very extensive studies on four peptides (alamethicin, melittin, magainin and proteg...
AbstractWe present an experimental study of the pore formation processes of small amphipathic peptid...
AbstractThe transition of the state of alamethicin from its inactive state to its active state of po...
We present an experimental study of the pore formation processes of small amphipathic peptides in mo...
ABSTRACT: Antimicrobial peptides are known to form pores in cell membranes. We study this process in...
AbstractRecently we have shown that the free energy for pore formation induced by antimicrobial pept...
AbstractRecently we have shown that the free energy for pore formation induced by antimicrobial pept...
The mechanism of pore formation of lytic peptides, such as melittin from bee venom, is thought to in...
Alamethicin is a transmembrane ion channel at low concentration, and a lytic agent of cell membrane ...
The mechanism of pore formation of lytic peptides, such as melittin from bee venom, is thought to in...
Adsorption of amphiphilic peptides to the headgroup region of a lipid bilayer is a common mode of pr...
Alamethicin adsorbs on the membrane surface at low peptide concentrations. However, above a critical...
Alamethicin adsorbs on the membrane surface at low peptide concentrations. However, above a critical...
Using dilatometry and small-angle X-ray diffraction, we have studied under bulk conditions the struc...
The mechanism of pore formation of lytic peptides, such as melittin from bee venom, is thought to in...
AbstractBased on very extensive studies on four peptides (alamethicin, melittin, magainin and proteg...
AbstractWe present an experimental study of the pore formation processes of small amphipathic peptid...
AbstractThe transition of the state of alamethicin from its inactive state to its active state of po...
We present an experimental study of the pore formation processes of small amphipathic peptides in mo...