How arginine derivatives alter the stability of lipid membranes: dissecting the roles of side chains, backbone and termini.

ABSTRACT: Arginine (R)-rich peptides constitute the most relevant class of cell-penetrating peptides and other membrane-active peptides that can translocate across the cell membrane or generate defects in lipid bilayers such as water-filled pores. The mode of action of R-rich peptides remains a topic of controversy, mainly because a quantitative and energetic understanding of arginine effects on membrane stability is lacking. Here, we explore the ability of several oligo-arginines R[Formula: see text] and of an arginine side chain mimic R[Formula: see text] to induce pore formation in lipid bilayers employing MD simulations, free-energy calculations, breakthrough force spectroscopy and leakage assays. Our experiments reveal that R[Formula: see text] but not R[Formula: see text] reduces the line tens

SUBMITTER: Verbeek SF 

PROVIDER: S-EPMC8071801 | biostudies-literature | 2021 Mar

REPOSITORIES: biostudies-literature