Effects of lactoferrin derived peptides on simulants of biological warfare agents

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• 作者：Tjitske Sijbrandij ; Antoon J. Ligtenberg…
• 关键词：Antimicrobial activity ; Antimicrobial peptide ; Biowarfare simulants ; Lactoferrin ; LFchimera
• 刊名：World Journal of Microbiology & Biotechnology
• 出版年：2017
• 出版时间：January 2017
• 年：2017
• 卷：33
• 期：1
• 全文大小：849 KB
• 刊物类别：Chemistry and Materials Science
• 刊物主题：Chemistry
  Applied Microbiology
  Biotechnology
  Biochemistry
  Environmental Biotechnology
  Microbiology
  
• 出版者：Springer Netherlands
• ISSN：1573-0972
• 卷排序：33

文摘

Lactoferrin (LF) is an important immune protein in neutrophils and secretory fluids of mammals. Bovine LF (bLF) harbours two antimicrobial stretches, lactoferricin and lactoferampin, situated in close proximity in the N1 domain. To mimic these antimicrobial domain parts a chimeric peptide (LFchimera) has been constructed comprising parts of both stretches (LFcin17–30 and LFampin265–284). To investigate the potency of this construct to combat a set of Gram positive and Gram negative bacteria which are regarded as simulants for biological warfare agents, the effect on bacterial killing, membrane permeability and membrane polarity were determined in comparison to the constituent peptides and the native bLF. Furthermore we aimed to increase the antimicrobial potency of the bLF derived peptides by cationic amino acid substitutions. Overall, the bactericidal activity of the peptides could be related to membrane disturbing effects, i.e. membrane permeabilization and depolarization. Those effects were most prominent for the LFchimera. Arginine residues were found to be crucial for displaying antimicrobial activity, as lysine to arginine substitutions resulted in an increased antimicrobial activity, affecting mostly LFampin265–284 whereas arginine to lysine substitutions resulted in a decreased bactericidal activity, predominantly in case of LFcin17–30.