TY - JOUR
T1 - Pseudin-2
T2 - An antimicrobial peptide with low hemolytic activity from the skin of the paradoxical frog
AU - Olson, Loyd
AU - Soto, Ana Maria
AU - Knoop, Floyd C.
AU - Conlon, J. Michael
PY - 2001/11/9
Y1 - 2001/11/9
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.
AB - 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.
KW - Amphibian skin
KW - Amphipathic α-helix
KW - Antimicrobial peptide
KW - Pseudidae
UR - http://www.scopus.com/inward/record.url?scp=0035834573&partnerID=8YFLogxK
U2 - 10.1006/bbrc.2001.5884
DO - 10.1006/bbrc.2001.5884
M3 - Article
C2 - 11689009
AN - SCOPUS:0035834573
SN - 0006-291X
VL - 288
SP - 1001
EP - 1005
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 4
ER -