Purification and properties of antimicrobial peptides from skin secretions of the Eritrea clawed frog Xenopus clivii (Pipidae)

详细信息    查看全文

• 作者：J. Michael Conlon^a ; ^{jmconlon@uaeu.ac.ae} ; Milena Mechkarska^a ; Eman Ahmed^a ; Jé ; rô ; me Leprince^b ; Hubert Vaudry^b ; Jay D. King^c ; Koji Takada^d
• 关键词：Antimicrobial peptide ; Frog skin ; Magainin ; Procaerulein ; Proxenopsin ; Antibiotic resistance
• 刊名：Comparative Biochemistry and Physiology, Part C
• 出版年：2011
• 出版时间：April 2011
• 年：2011
• 卷：153
• 期：3
• 页码：350-354
• 全文大小：367 K

文摘

Five peptides with antimicrobial activity were isolated from norepinephrine-stimulated skin secretions of the tetraploid frog Xenopus clivii Peracca, 1898 (Pipidae). Characterization of the peptides demonstrated that they are structurally similar to magainins (2 peptides), caerulein-precursor fragments, CPF (2 peptides), and xenopsin-precursor fragments, XPF (1 peptide) that have been previously isolated from other species of the genus Xenopus. The magainins and the XPF peptide were active only against the Gram-negative microorganism Escherichia coli whereas the CPF peptides were also active against the Gram-positive Staphylococcus aureus. The most abundant antimicrobial peptide in the secretions, CPF-C1 (GFGSLLGKALRLG ANVL.NH₂) inhibited the growth of the Gram-negative bacteria Acinetobacter baumannii, Klebsiella pneumoniae, and Pseudomonas aeruginosa (MIC ≤ 25 μM) suggesting potential for development into an anti-infective agent for use against these emerging antibiotic-resistant pathogens.