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

doi:10.1006/bbrc.2001.5884

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

Research output: Contribution to journal › Article › peer-review

48 Citations (Scopus)

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	https://doi.org/10.1006/bbrc.2001.5884
Publication status	Published - Nov 9 2001
Externally published	Yes

Keywords

Amphibian skin
Amphipathic α-helix
Antimicrobial peptide
Pseudidae

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1006/bbrc.2001.5884

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

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.",

keywords = "Amphibian skin, Amphipathic α-helix, Antimicrobial peptide, Pseudidae",

author = "Loyd Olson and Soto, {Ana Maria} and Knoop, {Floyd C.} and Conlon, {J. Michael}",

note = "Funding Information: 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).",

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doi = "10.1006/bbrc.2001.5884",

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AU - Soto, Ana Maria

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AU - Conlon, J. Michael

N1 - Funding Information: 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).

PY - 2001/11/9

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N2 - 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.

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

Abstract

Keywords

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