Peptide nanovesicles formed by the self-assembly of branched amphiphilic peptides

Abstract

Peptide-based packaging systems show great potential as safer drug delivery systems. They overcome problems associated with lipid-based or viral delivery systems, vis-a-vis stability, specificity, inflammation, antigenicity, and tune-ability. Here, we describe a set of 15 & 23-residue branched, amphiphilic peptides that mimic phosphoglycerides in molecular architecture. These peptides undergo supramolecular self-assembly and form solvent-filled, bilayer delimited spheres with 50–200 nm diameters as confirmed by TEM, STEM and DLS. Whereas weak hydrophobic forces drive and sustain lipid bilayer assemblies, these all-peptide structures are stabilized potentially by both hydrophobic interactions and hydrogen bonds and remain intact at low micromolar concentrations and higher temperatures. A linear peptide lacking the branch point showed no self-assembly properties. We have observed that these peptide vesicles can trap fluorescent dye molecules within their interior and are taken up by N/N 1003A rabbit lens epithelial cells grown in culture. These assemblies are thus potential drug delivery systems that can overcome some of the key limitations of the current packaging systems.

Description

Citation: Gudlur S, Sukthankar P, Gao J, Avila LA, Hiromasa Y, Chen J, et al. (2012) Peptide Nanovesicles Formed by the Self-Assembly of Branched Amphiphilic Peptides. PLoS ONE 7(9): e45374. https://doi.org/10.1371/journal.pone.0045374

Keywords

Peptide-based packaging systems, Drug delivery systems, Nanovesicles

Citation