Dimerization in tailoring uptake efficacy of the HSV-1 derived membranotropic peptide gH625

Sci Rep. 2017 Aug 25;7(1):9434. doi: 10.1038/s41598-017-09001-x.

Abstract

gH625 constitutes a promising delivery vehicle for the transport of therapeutic biomacromolecules across membrane barriers. We report an application of multivalency to create a complex nanosystem for delivery and to elucidate the mechanism of peptide-lipid bilayer interactions. Multivalency may offer a route to enhance gH625 cellular uptake as demonstrated by results obtained on dimers of gH625 by fluorescence spectroscopy, circular dichroism, and surface plasmon resonance. Moreover, using both phase contrast and light sheet fluorescence microscopy we were able to characterize and visualize for the first time the fusion of giant unilamellar vesicles caused by a membranotropic peptide.

MeSH terms

  • Amino Acid Sequence
  • Biological Transport
  • Cell Membrane / metabolism
  • Lipid Bilayers
  • Lipids / chemistry
  • Membrane Fluidity
  • Peptides / chemistry*
  • Peptides / metabolism
  • Protein Aggregates
  • Protein Binding
  • Protein Multimerization*
  • Surface Plasmon Resonance
  • Viral Envelope Proteins / chemistry*
  • Viral Envelope Proteins / metabolism*

Substances

  • Lipid Bilayers
  • Lipids
  • Peptides
  • Protein Aggregates
  • Viral Envelope Proteins
  • gH625 peptide, Herpes simplex virus type I