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Related Experiment Videos

Peptide stabilized amphotericin B nanodisks.

Megan Tufteland1, Joseph B Pesavento, Rachelle L Bermingham

  • 1Lipid Biology in Health and Disease Research Group, Children's Hospital Oakland Research Institute, 5700 Martin Luther King Jr. Way, Oakland, CA 94609, USA.

Peptides
|February 13, 2007
PubMed
Summary
This summary is machine-generated.

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A synthetic peptide effectively forms nanodisks (ND) with amphotericin B (AMB), matching the biological activity of those made with apolipoprotein A-I. This peptide offers a promising alternative for developing AMB nanodisks for clinical use.

Area of Science:

  • Biochemistry
  • Nanotechnology
  • Pharmacology

Background:

  • Nanodisks (ND) stabilized by apolipoprotein A-I (apoA-I) are used to formulate the antibiotic amphotericin B (AMB).
  • Investigating alternative components for ND formulation is crucial for optimizing drug delivery and clinical applications.

Purpose of the Study:

  • To evaluate if a synthetic peptide can replace the apolipoprotein component in forming and stabilizing AMB-loaded nanodisks (AMB-ND).
  • To compare the particle formation, stability, and biological activity of peptide-based AMB-ND with those formulated using apoA-I.

Main Methods:

  • Formulation of nanodisks using an 18-residue synthetic amphipathic alpha-helical peptide (4F) and various phospholipids.
  • Characterization of peptide-lipid interactions using tryptophan fluorescence spectroscopy.

Related Experiment Videos

  • Preparation and characterization of 4F AMB-ND using negative stain electron microscopy.
  • Assessment of antifungal activity of 4F AMB-ND compared to apoA-I AMB-ND in growth inhibition assays.

    • Main Results:

    • The synthetic peptide 4F efficiently solubilized phospholipid vesicles, comparable to apoA-I.
    • Interaction with lipids induced significant changes in 4F's tryptophan fluorescence, indicating structural changes.
    • Negative stain electron microscopy confirmed that 4F AMB-ND formed stable, disk-shaped particles similar to apoA-I AMB-ND.
    • The 4F AMB-ND demonstrated potent antifungal activity against yeast and pathogenic fungi, equivalent to apoA-I AMB-ND.

    Conclusions:

    • An 18-residue synthetic amphipathic peptide can effectively form stable, disk-shaped nanodisks with amphotericin B.
    • Peptide-based AMB-ND exhibit potent biological activity comparable to those formulated with apolipoprotein A-I.
    • Peptides represent a versatile and potentially advantageous alternative to apolipoprotein A-I for the scale-up and clinical application of AMB-ND.