5 years ago

Peptide–Membrane Interaction between Targeting and Lysis

Peptide–Membrane Interaction between Targeting and Lysis
Gernot Posselt, Gil Kanfer, Katharina Stutz, Silja Wessler, Petra Schneider, Paul Wrede, Jan A. Hiss, Bernhard Pfeiffer, Markus Blatter, Alex T. Müller, Gisbert Schneider, Karl-Heinz Altmann, Benoît Kornmann
Certain cationic peptides interact with biological membranes. These often-complex interactions can result in peptide targeting to the membrane, or in membrane permeation, rupture, and cell lysis. We investigated the relationship between the structural features of membrane-active peptides and these effects, to better understand these processes. To this end, we employed a computational method for morphing a membranolytic antimicrobial peptide into a nonmembranolytic mitochondrial targeting peptide by “directed simulated evolution.” The results obtained demonstrate that superficially subtle sequence modifications can strongly affect the peptides’ membranolytic and membrane-targeting abilities. Spectroscopic and computational analyses suggest that N- and C-terminal structural flexibility plays a crucial role in determining the mode of peptide–membrane interaction.

Publisher URL: http://dx.doi.org/10.1021/acschembio.7b00504

DOI: 10.1021/acschembio.7b00504

You might also like
Discover & Discuss Important Research

Keeping up-to-date with research can feel impossible, with papers being published faster than you'll ever be able to read them. That's where Researcher comes in: we're simplifying discovery and making important discussions happen. With over 19,000 sources, including peer-reviewed journals, preprints, blogs, universities, podcasts and Live events across 10 research areas, you'll never miss what's important to you. It's like social media, but better. Oh, and we should mention - it's free.

  • Download from Google Play
  • Download from App Store
  • Download from AppInChina

Researcher displays publicly available abstracts and doesn’t host any full article content. If the content is open access, we will direct clicks from the abstracts to the publisher website and display the PDF copy on our platform. Clicks to view the full text will be directed to the publisher website, where only users with subscriptions or access through their institution are able to view the full article.