Novel short antimicrobial peptide isolated from Xenopus laevis skin

作者：Zhang, Yu; Liu, Songcai; Li, Siming; Cheng, Yunyun; Nie, Linyan; Wang, Gang; Lv, Chen; Wei, Wenzhen; Cheng, Cheng; Hou, Feng^*; Hao, Linlin^*

来源：Journal of Peptide Science, 2017, 23(5): 403-409.

DOI：10.1002/psc.2990

• antimicrobial peptides
• Xenopus laevis
• antimicrobial characterisation
• cell haemolysis

A rich source of bioactive peptides, including a large number of antimicrobial peptides, has been found in amphibian skin. In this study, a novel short antimicrobial peptide was purified from Xenopus laevis skin and characterised through reversed-phase high-performance liquid chromatography, Edman degradation and matrix-assisted laser desorption/ionisation time-of-flight mass spectrometry. The peptide was composed of six amino acids with a sequence of DEDLDE and thus named X. laevis antibacterial peptide-P2 (XLAsp-P2). Transmission electron microscopy revealed that this peptide showed potential antimicrobial abilities against bacteria by damaging the bacterial cell membrane. XLAsp-P2 maybe inhibit bacterial growth by binding to the microbial genomic DNA. The peptide also exhibited a weak haemolytic activity against rabbit red blood cells. Therefore, XLAsp-P2 is a novel short anionic antibacterial peptide with broad activities.

• 出版日期2017-5
• 单位吉林大学