Lipid-like self-assembling peptide nanovesicles for drug delivery

Dimitrios G. Fatouros, Dimitrios A. Lamprou, Andrew Urquhart, Spyros N. Yannopoulos, Ioannis S. Vizirianakis, Shuguang Zhang, Sotirios Koutsopoulos

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

Amphiphilic self-assembling peptides are functional materials, which, depending on the amino acid sequence, the peptide length, and the physicochemical conditions, form a variety of nanostructures including nanovesicles, nanotubes, and nanovalves. We designed lipid-like peptides with an aspartic acid or lysine hydrophilic head and a hydrophobic tail composed of six alanines (i.e., ac-A6K-CONH2, KA6-CONH2, ac-A6D-COOH, and DA6-COOH). The resulting novel peptides have a length similar to biological lipids and form nanovesicles at physiological conditions. AFM microscopy and light scattering analyses of the positively charged lipid-like ac-A6K-CONH2, KA6-CONH2 peptide formulations showed individual nanovesicles. The negatively charged ac-A6D-COOH and DA6-COOH peptides self-assembled into nanovesicles that formed clusters that upon drying were organized into necklace-like formations of nanovesicles. Encapsulation of probe molecules and release studies through the peptide bilayer suggest that peptide nanovesicles may be good candidates for sustained release of pharmaceutically active hydrophilic and hydrophobic compounds. Lipid-like peptide nanovesicles represent a paradigm shifting system that may complement liposomes for the delivery of diagnostic and therapeutic agents. © 2014 American Chemical Society.
Original languageEnglish
JournalA C S Applied Materials and Interfaces
Volume6
Issue number11
Pages (from-to)8184-8189
Number of pages6
ISSN1944-8244
DOIs
Publication statusPublished - 2014
Externally publishedYes

Keywords

  • controlled release
  • designer peptide surfactants
  • lipid-like peptides
  • liposome alternatives
  • tunable peptides
  • Amino acids
  • Drug delivery
  • Functional materials
  • Hydrophilicity
  • Hydrophobicity
  • Liposomes
  • Amino acid sequence
  • Controlled release
  • Hydrophilic and hydrophobic
  • Lipid-like peptides
  • Physicochemical conditions
  • Physiological condition
  • Scattering analysis
  • Self-assembling peptides
  • Peptides

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