Journal
JOURNAL OF PEPTIDE RESEARCH
Volume 62, Issue 5, Pages 207-213Publisher
WILEY
DOI: 10.1034/j.1399-3011.2003.00090.x
Keywords
amphibian skin; brevinin-1; Candida albicans; Rana; ranatuerin-2; temporin
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The emergence of strains of the human pathogen Candida albicans with resistance to commonly used antibiotics has necessitated a search for new types of antifungal agents. Six peptides with antimicrobial activity were isolated from norepinephrine-stimulated skin secretions from the foothill yellow-legged frog Rana boylii. Brevinin-1BYa (FLPILASLAA(10)KFGPKLF (CLVTKKC)-T-20) was particularly potent against C albicans [minimal inhibitory concentration (MIC) = 3 muM] and also active against Escherichia coli (MIC 17 muM) and Staphylococcus aureus (MIC = 2 muM), but its therapeutic potential for systemic use is limited by its strong hemolytic activity (HC50 = 4 muM). The single amino acid substitution (Phe(12) --> Leu) in brevinin-1BYb resulted in a fourfold lower potency against C albicans and the additional amino acid substitutions (Lys(11) --> Thr, Phe(17) --> Leu and Val(20) --> Ile) in brevinin-1BYc resulted in a ninefold decrease in activity. Two members of the ranatuerin-2 family and one member of the temporin family were also isolated from the secretions but showed relatively low potency against the three microorganisms tested.
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