title: Brevinin-1BYa: a naturally occurring peptide from frog skin with broad-spectrum antibacterial and antifungal properties.
abstract: Brevinin-1BYa (FLPILASLAAKFGPKLFCLVTKKC) is a cationic alpha-helical peptide containing an intramolecular disulphide bridge that is present in skin secretions of the foothill yellow-legged frog Rana boylii. A synthetic replicate of the peptide showed growth inhibitory activity against a range of reference strains of Gram-positive and Gram-negative bacteria, against clinical isolates of methicillin-resistant Staphylococcus aureus (MRSA) (minimum inhibitory concentration (MIC)=2.5 microM), and against reference strains and clinical isolates of the opportunistic yeast pathogens Candida albicans, Candida tropicalis, Candida krusei and Candida parapsilosis (MIC<or=10 microM). However, the therapeutic potential of the peptide, especially for systemic applications, is restricted by its high haemolytic activity against human erythrocytes (LD50=10 microM). Replacement of the cysteine residues in brevinin-1BYa by serine produced an acyclic analogue with eight-fold reduced haemolytic activity that retained high potency against Gram-positive bacteria, including strains of MRSA (MIC=5 microM), however activities against Gram-negative bacteria and yeast species were reduced. It is suggested that brevinin-1BYa represents a candidate for drug development, particularly for topical applications against antibiotic-resistant microorganisms.
authors.affiliation: Department of Medical Microbiology, Faculty of Medicine and Health Sciences, United Arab Emirates University, 17666 Al-Ain, United Arab Emirates.
authors.forename: Tibor
authors.initials: T
authors.lastname: Pál
authors.forename: Bency
authors.initials: B
authors.lastname: Abraham
authors.forename: Agnes
authors.initials: A
authors.lastname: Sonnevend
authors.forename: Pauline
authors.initials: P
authors.lastname: Jumaa
authors.forename: J Michael
authors.initials: JM
authors.lastname: Conlon
mesh_terms: D000595:Amino Acid Sequence; D029845:Amphibian Proteins / Q000494:pharmacology*; D000900:Anti-Bacterial Agents / Q000494:pharmacology*; D000935:Antifungal Agents / Q000494:pharmacology*; D023181:Antimicrobial Cationic Peptides / Q000494:pharmacology*; D008826:Microbial Sensitivity Tests; D008969:Molecular Sequence Data
chemical_list: D029845:Amphibian Proteins; D000900:Anti-Bacterial Agents; D000935:Antifungal Agents; D023181:Antimicrobial Cationic Peptides; C078413:brevinin-1 protein, Rana