Peptide self-assembly into lamellar phases and the formation of lipid-peptide nanostructures.

ABSTRACT: Lipids exhibit an extraordinary polymorphism in self-assembled mesophases, with lamellar phases as biologically most relevant representative. To mimic lipid lamellar phases with amphiphilic designer peptides, seven systematically varied short peptides were engineered. Indeed, four peptide candidates (V₄D, V₄WD, V₄WD₂, I₄WD₂) readily self-assembled into lamellae in aqueous solution: small-angle X-ray scattering patterns (SAXS) revealed ordered lamellar structures with a repeat distance of ~4-5 nm. Transmission electron microscopy (TEM) images confirmed the presence of stacked sheets. Two derivatives (V₃D and V₄D₂) remained as loose aggregates dispersed in solution; one peptide (L₄WD

SUBMITTER: Kornmueller K 

PROVIDER: S-EPMC5777605 | biostudies-literature | 2018 Feb

REPOSITORIES: biostudies-literature