The maculatin peptides from the skin glands of the tree frog Litoria genimaculata: a comparison of the structures and antibacterial activities of maculatin 1.1 and caerin 1.1

J Pept Sci. 1998 Apr;4(2):111-5. doi: 10.1002/(sici)1099-1387(199804)4:2<111::aid-psc134>3.0.co;2-8.

Abstract

Six peptides have been isolated and characterized from the dorsal glands of the tree frog Litoria genimaculata. One of these is the known hypotensive peptide caerulein; the others have been named maculatins. The amino acid sequences of the maculatin peptides have been determined using a combination of fast atom bombardment mass spectrometry and automated Edman sequencing. Four of the maculatin peptides show antibiotic activity, with maculatin 1.1 [GLFGVLAKVAAHVVPAIAEHF(NH2)] showing the most pronounced activity, particularly against gram-positive organisms. Maculatin 1.1 resembles the known caerin 1 antibiotic peptides, except that four of the central amino acid residues (of the caerin 1 system) are missing in maculatin 1.1. A comparison of the antibiotic activity of maculatin 1.1 with those of caerin 1.1 is reported.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Amphibian Proteins*
  • Animals
  • Anti-Bacterial Agents / chemistry*
  • Anti-Infective Agents / chemistry
  • Anti-Infective Agents / pharmacology
  • Antimicrobial Cationic Peptides*
  • Anura
  • Australia
  • Mass Spectrometry
  • Molecular Sequence Data
  • New Guinea
  • Peptides / chemistry*
  • Sequence Analysis
  • Skin / chemistry*

Substances

  • Amphibian Proteins
  • Anti-Bacterial Agents
  • Anti-Infective Agents
  • Antimicrobial Cationic Peptides
  • Peptides
  • caerin 1.1, Anura
  • maculatin-1.1 protein, Litoria