Ocellatins: new antimicrobial peptides from the skin secretion of the South American frog Leptodactylus ocellatus (Anura: Leptodactylidae).
The emergence, in recent years, of microbial resistance to commonly used antibiotics has aroused a search for new naturally occurring bactericidal and fungicidal agents that may have clinical utility. In the present study, three new antimicrobial peptides were purified from the electrical-stimulated skin secretion of the South American frog Leptodactylus ocellatus by reversed-phase chromatographic procedures. Ocellatin 1 (1GVVDILKGAGKDLLAHLVGKISEKV25-CONH2), ocellatin 2 (1GVLDIFKDAAKQILAHAAEKQI25-CONH2) and ocellatin 3 (1GVLDILKNAAKNILAHAAEQI21-CONH2) are structurally related peptides. These peptides present hemolytic activity against human erythrocytes and are also active against Escherichia coli. Ocellatins exhibit significant sequence similarity to other amphibian antimicrobial peptides, mainly to brevinin 2ED from Rana esculenta.
Nascimento
Anna Christina C
AC
Toxinology Laboratory, Department of Physiological Sciences, University of Brasilia, Brasilia/DF, Brazil, 70.910-900.
Zanotta
Lanuse C
LC
Kyaw
Cynthia M
CM
Schwartz
Elisabeth N F
EN
Schwartz
Carlos A
CA
Sebben
Antonio
A
Sousa
Marcelo V
MV
Fontes
Wagner
W
Castro
Mariana S
MS
D000595:Amino Acid Sequence; D000818:Animals; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry / Q000302:isolation & purification*; D001001:Anura; D002851:Chromatography, High Pressure Liquid; D004926:Escherichia coli / Q000187:drug effects; D006461:Hemolysis / Q000187:drug effects; D006801:Humans; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D016415:Sequence Alignment; D012867:Skin / Q000378:metabolism*
D023181:Antimicrobial Cationic Peptides; D010455:Peptides; C500819:ocellatin 1 protein, Leptodactylus ocellatus; C500820:ocellatin 2 protein, Leptodactylus ocellatus; C500821:ocellatin 3 protein, Leptodactylus ocellatus