Antiviral cyclic D,L-alpha-peptides: targeting a general biochemical pathway in virus infections

Bioorg Med Chem. 2005 Sep 1;13(17):5145-53. doi: 10.1016/j.bmc.2005.05.051.

Abstract

Diverse virus families have evolved to exploit the acidification of endosomal compartments to gain entry into cells. We describe a supramolecular approach for selectively targeting and inhibiting viral infections through this central biochemical pathway. Using adenovirus as a model non-enveloped virus, we have determined that an eight-residue cyclic D,L-alpha-peptide, selected from a directed combinatorial library, can specifically prevent the development of low pH in endocytic vesicles, arrest the escape of virions from the endosome, and abrogate adenovirus infection without an apparent adverse effect on cell viability. The likely generality of this approach against other pH-dependent viral infections is supported by the inhibition of type-A influenza virus escape from endosomes in the presence of the same peptide. Our studies suggest that self-assembling cyclic D,L-alpha-peptides hold considerable potential as a new rational supramolecular approach toward the design and discovery of broad-spectrum antiviral agents.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Antiviral Agents / chemistry
  • Antiviral Agents / pharmacology*
  • Antiviral Agents / therapeutic use
  • Cell Line
  • Dogs
  • Fluorescent Dyes
  • Humans
  • Peptides, Cyclic / chemistry
  • Peptides, Cyclic / pharmacology*
  • Peptides, Cyclic / therapeutic use
  • Spectroscopy, Fourier Transform Infrared
  • Virus Diseases / drug therapy*

Substances

  • Antiviral Agents
  • Fluorescent Dyes
  • Peptides, Cyclic