Lipid-like self-assembling peptide nanovesicles for drug delivery

D G Fatouros, Dimitrios Lamprou, Andrew Urquhart, Spyros Yannopoulos, Ioannis Vizirianakis, Shuguang Zhang, Sotirios Koutsopoulos

Research output: Contribution to journalArticle

43 Citations (Scopus)

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 comprised 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 which 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.
LanguageEnglish
Pages8184–8189
Number of pages6
JournalACS Applied Materials and Interfaces
Volume6
Issue number11
Early online date12 May 2014
DOIs
Publication statusPublished - 2014

Fingerprint

Drug delivery
Lipids
Peptides
Pharmaceutical Preparations
Nanotubes
Functional materials
Nanostructures
Liposomes
Encapsulation
Aspartic Acid
Alanine
Light scattering
Lysine
Amino acids
Microscopy
Amino Acid Sequence
Drying
Microscopic examination
Head
Light

Keywords

  • lipid-like
  • self assembling
  • peptide nanovesicles
  • drug delivery

Cite this

Fatouros, D. G., Lamprou, D., Urquhart, A., Yannopoulos, S., Vizirianakis, I., Zhang, S., & Koutsopoulos, S. (2014). Lipid-like self-assembling peptide nanovesicles for drug delivery. ACS Applied Materials and Interfaces, 6(11), 8184–8189. https://doi.org/10.1021/am501673x
Fatouros, D G ; Lamprou, Dimitrios ; Urquhart, Andrew ; Yannopoulos, Spyros ; Vizirianakis, Ioannis ; Zhang, Shuguang ; Koutsopoulos, Sotirios. / Lipid-like self-assembling peptide nanovesicles for drug delivery. In: ACS Applied Materials and Interfaces. 2014 ; Vol. 6, No. 11. pp. 8184–8189.
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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 comprised 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 which 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.",
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Fatouros, DG, Lamprou, D, Urquhart, A, Yannopoulos, S, Vizirianakis, I, Zhang, S & Koutsopoulos, S 2014, 'Lipid-like self-assembling peptide nanovesicles for drug delivery' ACS Applied Materials and Interfaces, vol. 6, no. 11, pp. 8184–8189. https://doi.org/10.1021/am501673x

Lipid-like self-assembling peptide nanovesicles for drug delivery. / Fatouros, D G; Lamprou, Dimitrios; Urquhart, Andrew; Yannopoulos, Spyros; Vizirianakis, Ioannis; Zhang, Shuguang; Koutsopoulos, Sotirios.

In: ACS Applied Materials and Interfaces, Vol. 6, No. 11, 2014, p. 8184–8189.

Research output: Contribution to journalArticle

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T1 - Lipid-like self-assembling peptide nanovesicles for drug delivery

AU - Fatouros, D G

AU - Lamprou, Dimitrios

AU - Urquhart, Andrew

AU - Yannopoulos, Spyros

AU - Vizirianakis, Ioannis

AU - Zhang, Shuguang

AU - Koutsopoulos, Sotirios

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N2 - 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 comprised 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 which 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.

AB - 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 comprised 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 which 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.

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Fatouros DG, Lamprou D, Urquhart A, Yannopoulos S, Vizirianakis I, Zhang S et al. Lipid-like self-assembling peptide nanovesicles for drug delivery. ACS Applied Materials and Interfaces. 2014;6(11):8184–8189. https://doi.org/10.1021/am501673x