Nanodisc-to-Nanofiber Transition of Noncovalent Peptide-Phospholipid Assemblies.

ABSTRACT: We report a novel molecular architecture of peptide-phospholipid coassemblies. The amphiphilic peptide Ac-18A-NH₂ (18A), which was designed to mimic apolipoprotein α-helices, has been shown to form nanodisc structures with phospholipid bilayers. We show that an 18A peptide cysteine substitution at residue 11, 18A[A11C], forms fibrous assemblies with 1-palmitoyl-2-oleoyl-phosphatidylcholine at a lipid-to-peptide (L/P) molar ratio of 1, a fiber diameter of 10-20 nm, and a length of more than 1 μm. Furthermore, 18A[A11C] can form nanodiscs with these lipid bilayers at L/P ratios of 4-6. The peptide adopts α-helical structures in both the nanodisc and nanofiber assemblies, although the α-helical bundle structures were evident only in the nanofibers, and the phospholipids of the nano

SUBMITTER: Ikeda K 

PROVIDER: S-EPMC6641012 | biostudies-literature | 2017 Jun

REPOSITORIES: biostudies-literature