The amphipathic alpha-helix concept - application to the de-novo design of ideally amphipathic Leu, Lys peptides with hemolytic-activity higher than that of melittin
Structure-antitumor and hemolytic activity relationships of synthetic peptides derived from cecropin A magainin 2 and cecropin A melittin hybrid peptides
Structural identification by mass spectrometry of a novel antimicrobial peptide from the venom of the solitary bee Osmia rufa (Hymenoptera: Megachilidae)
Structural and charge requirements for antimicrobial and hemolytic-activity in the peptide Pklletflskwig, corresponding to the hydrophobic region of the antimicrobial protein bovine seminal plasmin
Sitaram, N.Int. J. Pept. Prot. Res 46 166-173[1995]
Structural and biological characterization of two novel peptides from the venom of the neotropical social wasp Agelaia pallipes pallipes
Peptide helicity and membrane surface charge modulate the balance of electrostatic and hydrophobic interactions with lipid bilayers and biological membranes
Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membranelytic peptides
Investigating the effect of different positioning of lysine residues along the peptide chain of mastoparans for their secondary structures and biological activities
Effects of net charge and the number of positively charged residues on the biological activity of amphipathic alpha-helical cationic antimicrobial peptides
Dominulin A and B: two new antibacterial peptides identified on the cuticle and in the venom of the social paper wasp Polistes dominulus using MALDI-TOF, MALDI-TOF/TOF, and ESI-ion trap
Design and synthesis of amphiphilic alpha-helical model peptides with systematically varied hydrophobic-hydrophilic balance and their interaction with lipid- and bio-membranes