An amphipathic alpha-helical peptide from apolipoprotein A1 stabilizes protein polymer vesicles.

ABSTRACT: L4F, an alpha helical peptide inspired by the lipid-binding domain of the ApoA1 protein, has potential applications in the reduction of inflammation involved with cardiovascular disease as well as an antioxidant effect that inhibits liver fibrosis. In addition to its biological activity, amphipathic peptides such as L4F are likely candidates to direct the molecular assembly of peptide nanostructures. Here we describe the stabilization of the amphipathic L4F peptide through fusion to a high molecular weight protein polymer. Comprised of multiple pentameric repeats, elastin-like polypeptides (ELPs) are biodegradable protein polymers inspired from the human gene for tropoelastin. Dynamic light scattering confirmed that the fusion peptide forms nanoparticles with a hydrodynamic radius of appro

SUBMITTER: Pastuszka MK 

PROVIDER: S-EPMC4327866 | biostudies-literature | 2014 Oct

REPOSITORIES: biostudies-literature