Membrane proteins perform a host of vital cellular functions. Deciphering the molecular
mechanisms whereby they fulfill these functions requires detailed biophysical and structural …

Antimicrobial peptides are ancient components of the innate immune system and have been
isolated from organisms spanning the phylogenetic spectrum. Over an evolutionary time …

We review the fundamental strategies used by small peptides to associate with lipid
membranes and how the different strategies impact on the structure and dynamics of the …

Antimicrobial peptides (AMPs) attack bacterial membranes selectively, killing microbes at
concentrations that cause no toxicity to the host cells. This selectivity is not due to interaction …

Antimicrobial peptides (AMPs), important effector molecules of the innate immune system,
also provide templates for designing novel antibiotics. Protegrin, an especially potent AMP …

Naturally occurring and synthetic peptides may be a novel class of clinically useful
antibiotics. A large body of experimental data on structure function relationships for such …

Antimicrobial peptides (AMPs) are promising candidates for the development of future
antibiotics. In an attempt to increase the efficacy of therapeutic AMPs, computer-based …

The increase in multidrug resistant bacteria has sparked an interest in the development of
novel antibiotics. Antimicrobial peptides that operate by crossing the cell membrane may …

Previous optimisation studies of peptide/peptoid hybrids typically comprise comparison of
structurally related analogues displaying different oligomer length and diverse side chains …

Recently, we reported a cationic 14 residue peptide LL-14 (LKWLKKLLKWLKKL) with salt-
sensitive broad-spectrum antimicrobial potency. However, the mechanism of its salt (NaCl) …