The solution structure of uperin 3.6, an antibiotic peptide from the granular dorsal glands of the Australian toadlet, Uperoleia mjobergii

J Pept Res. 1999 Aug;54(2):137-45. doi: 10.1034/j.1399-3011.1999.00095.x.

Abstract

Uperin 3.6 (GVIDA5AKKVV10NVLKN15LF-NH2) is a wide-spectrum antibiotic peptide isolated from the Australian toadlet, Uperoleia mjobergii. With only 17 amino acid residues, it is smaller than most other wide-spectrum antibiotic peptides isolated from amphibians. In 50% (by vol.) trifluoroethanol, an NMR study and structure calculations indicate that uperin 3.6 adopts a well-defined amphipathic alpha-helix with distinct hydrophilic and hydrophobic faces. Examination of the activities of synthetic modifications of uperin 3.6 reveal that the three lysine residues are essential for antibiotic activity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Amphibian Proteins
  • Animals
  • Anti-Bacterial Agents / chemistry*
  • Anura
  • Circular Dichroism
  • Magnetic Resonance Spectroscopy
  • Molecular Sequence Data
  • Peptides*
  • Protein Conformation
  • Proteins / chemistry*
  • Skin / chemistry*

Substances

  • Amphibian Proteins
  • Anti-Bacterial Agents
  • Peptides
  • Proteins
  • uperin 3.6 peptide, Uperoleia mjobergii