ACTA VETERINARIA ET ZOOTECHNICA SINICA ›› 2013, Vol. 44 ›› Issue (7): 1124-1130.doi: 10.11843/j.issn.0366-6964.2013.07.018

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The Action Mechanism of Two Analogues of the Antimicrobial Peptide BuforinⅡ on Staphylococcus aureus Membrane

HAO Gang1, LE Guo-wei2, SHI Yong-hui2   

  1. (1. College of Life Science and Technology, Southwest University for Nationalities, Chengdu 610041, China; 2. School of Food Science and Technology, Jiangnan University, Wuxi 214122, China)
  • Received:2012-11-29 Online:2013-07-23 Published:2013-07-23

Abstract:

In this paper, the action mechanism of BF2-A/B, two analogues of antimicrobial peptide Buforin, on Staphylococcus aureus membrane had been researched. The results of FACScan analysis implied that BF2-A/B did not induce the influx of PI into the S. aureus cells. The rate of positive cells stained by fluorescent probe after BF2-B treatment was slightly higher than that of BF2-A. These electron micrographs showed that after 20 min of treatment by BF2-A, S. aureus cells still retained the plasma membrane integrality; however, BF2-B could cause some slight leakages of cellular cytoplasmic contents. The results of FACS analysis displayed that both the peptides could penetrate the cells, and BF2-B penetrated the cells more efficiently. The visualization of confocal microscopy proved that FITC-labeled BF2-A and BF2-B penetrated the bacterial cell membrane and accumulated in the cytoplasm of the cell immediately. The results of research demonstrated that BF2-A/B didnt destroy the cell membrane of G+ bacteria, and then exert the antimicrobial activity after influx into cytoplasm. BF2-B slightly disturbed cell membrane causing influx of PI and leakage of cytoplasmic contents during peptide crossing phospholipids bilayer. Meanwhile, the cell-penetrating efficiency of BF2-B was accordingly enhanced, which caused that BF2-B displayed more excellent antimicrobial activity to S. aureus.

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