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• W2064548897 abstract "Nine peptides with differential growth inhibitory activity against Escherichia coli and Staphylococcus aureus were isolated from norepinephrine-stimulated skin secretions of the tetraploid frog Xenopus borealis Parker, 1936 (Pipidae). Structural characterization of the peptides demonstrated that they were orthologous to magainin-2 (1 peptide), peptide glycine–leucine-amide, PGLa (2 peptides), caerulein-precursor fragments, CPF (4 peptides), and xenopsin-precursor fragments, XPF (2 peptides), previously isolated from Xenopus laevis and X. amieti. In addition, a second magainin-related peptide (G**KFLHSAGKFGKAFLGEVMIG) containing a two amino acid residue deletion compared with magainin-2 was identified that had only weak antimicrobial activity. The peptide with the greatest potential for development into a therapeutically valuable anti-infective agent was CPF-B1 (GLGSLLGKAFKIGLKTVGKMMGGAPREQ) with MIC = 5 μM against E. coli, MIC = 5 μM against S. aureus, and MIC = 25 μM against Candida albicans, and low hemolytic activity against human erythrocytes (LC50 > 200 μM). This peptide was also the most abundant antimicrobial peptide in the skin secretions. CPF-B1 was active against clinical isolates of the nosocomial pathogens, methicillin-resistant S. aureus (MRSA) and multidrug-resistant Acinetobacter baumannii (MDRAB) with MIC values in the range 4–8 μM." @default.
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• W2064548897 date "2010-11-01" @default.
• W2064548897 modified "2023-10-06" @default.
• W2064548897 title "Antimicrobial peptides with therapeutic potential from skin secretions of the Marsabit clawed frog Xenopus borealis (Pipidae)" @default.
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• W2064548897 doi "https://doi.org/10.1016/j.cbpc.2010.07.007" @default.
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