Abstract
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 language | English |
|---|---|
| Pages (from-to) | 1001-1005 |
| Number of pages | 5 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 288 |
| Issue number | 4 |
| DOIs | |
| Publication status | Published (in print/issue) - 9 Nov 2001 |
Funding
We thank Dr. Donald Babin, Creighton University, for amino acid analyses; Ms. Eva Lovas, Creighton University, for mass spectrometry measurements; and Dr. Luis Marky, University of Nebraska Medical Center, Omaha, for providing facilities for CD spectroscopy. This work was supported by Restoragen Inc. (Lincoln, NE).
| Funder number |
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| NE |
Keywords
- Amphibian skin
- Amphipathic α-helix
- Antimicrobial peptide
- Pseudidae
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