Membrane permeabilizing peptides (MPPs) are as ubiquitous as the lipid bilayer
membranes they act upon. Produced by all forms of life, most membrane permeabilizing …

The biogenesis, folding, and structure of α-helical membrane proteins (MPs) are important to
understand because they underlie virtually all physiological processes in cells including key …

In the age of failing small-molecule antibiotics, tapping the near-infinite structural and
chemical repertoire of antimicrobial peptides (AMPs) offers one of the most promising routes …

Membrane active peptides are known to porate lipid bilayers, but their exact
permeabilization mechanism and the structure of the nanoaggregates they form in …

Antimicrobial peptides (AMPs), as a key component of the immune defense systems of
organisms, are a promising solution to the serious threat of drug-resistant bacteria to public …

Many antimicrobial peptides (AMPs) selectively target and form pores in microbial
membranes. However, the mechanisms of membrane targeting, pore formation and function …

Melittin (MEL), a small peptide component of bee venom, has been reported to exhibit anti-
cancer effects in vitro and in vivo. However, its clinical applicability is disputed because of its …

The determination of membrane protein (MP) structures has always trailed that of soluble
proteins due to difficulties in their overexpression, reconstitution into membrane mimetics …

Lyme disease is a tick-borne, multi-systemic disease, caused by the bacterium Borrelia
burgdorferi. Though antibiotics are used as a primary treatment, relapse often occurs after …

Membrane-active antimicrobial peptides (AMPs) are challenging to study experimentally, but
relatively easy to investigate using molecular dynamics (MD) computer simulations. For this …