The interactions of cationic amphipathic antimicrobial peptides (AMPs) with anionic
biological membranes have been the focus of much research aimed at improving the activity …

The interaction of antimicrobial peptides (AMPs) with the inner membrane of Gram-negative
bacteria is a key determinant of their abilities to exert diverse bactericidal effects. Here we …

Even 30 years after the discovery of magainins, biophysical and structural investigations on
how these peptides interact with membranes can still bear surprises and add new …

Novel cationic antimicrobial peptides (CAPs) designed in our lab—typified by sequences
such as KKKKKKAAX‐AAXAAXAA‐NH2, where X= Phe/Trp—display high antibacterial …

Combining two known antimicrobial peptides (AMPs) into a hybrid peptide is one promising
avenue in the design of agents with increased antibacterial activity. However, very few …

The innate immunity of multicellular organisms relies in large part on the action of
antimicrobial peptides (AMPs) to resist microbial invasion. Crafted by evolution into an …

Amphipathic peptides are accommodated within the diffuse gradient of polarity that
characterizes the interfacial regions of phospholipid bilayer membranes. Interfacial …

Membrane-active peptides exhibit a wide variety of biological functions including pore
formation, signaling and antimicrobial activities. They are also capable of transporting large …

Membranes are a central feature of all biological systems, and their ability to control many
cellular processes is critically important. As a result, a better understanding of how …

Abstract Brevinin‐1BYa (FLPILASLAAKFGPKLFCLVTKKC), first isolated from skin
secretions of the foothill yellow‐legged frog Rana boylii, shows broad‐spectrum activity …