Pseudin-2: An antimicrobial peptide with low hemolytic activity from the skin of the paradoxical frog

Loyd Olson, Ana Maria Soto, Floyd C. Knoop, J. Michael Conlon

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47 Citations (Scopus)


Four structurally related peptides (pseudins 1-4) with antimicrobial activity were isolated from an extract of the skin of the paradoxical frog Pseudis paradoxa (Pseudidae). Pseudin-2 (GLNALKKVFQGIHEAIKLINNHVQ) was the most abundant peptide (22 nmol/g tissue) and also the most potent (minimum inhibitory concentrations, MIC = 2.5 μM against Escherichia coli, 80 μM against Staphylococcus aureus, and 130 μM against Candida albicans). The concentration of pseudin-2 producing 50% hemolysis of human erythrocytes was >300 μM. Circular dichroism studies showed that the pseudins belong to the class of cationic, amphipathic α-helical antimicrobial peptides but their amino acid sequences are not similar to any previously characterized peptides from frog skin. The pseudins do, however, show sequence similarity with a region at the C-terminus of DEFT, a death effector domain-containing protein expressed in mammalian testicular germ cells that is involved in the regulation of apoptosis.

Original languageEnglish
Pages (from-to)1001-1005
Number of pages5
JournalBiochemical and Biophysical Research Communications
Issue number4
Publication statusPublished - Nov 9 2001
Externally publishedYes


  • Amphibian skin
  • Amphipathic α-helix
  • Antimicrobial peptide
  • Pseudidae

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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