Influence of Dimerization of Lipopeptide Laur-Orn-Orn-Cys–NH2 and an N-terminal Peptide of Human Lactoferricin on Biological Activity
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  • 作者:El?bieta Kamysz ; Emilia Sikorska…
  • 关键词:Antimicrobial activity ; Circular dichroism ; Haemolytic activity ; Lactoferricin ; Lactoferrin ; Lipopeptide
  • 刊名:International Journal of Peptide Research and Therapeutics
  • 出版年:2015
  • 出版时间:March 2015
  • 年:2015
  • 卷:21
  • 期:1
  • 页码:39-46
  • 全文大小:1,164 KB
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  • 作者单位:El?bieta Kamysz (1)
    Emilia Sikorska (1)
    Ma?gorzata Dawgul (2)
    Rafa? Tyszkowski (1)
    Wojciech Kamysz (2)

    1. Faculty of Chemistry, University of Gdańsk, Wita Stwosza 63, 80-308, Gdańsk, Poland
    2. Faculty of Pharmacy, Medical University of Gdańsk, Al. Gen. Hallera 107, 80-416, Gdańsk, Poland
  • 刊物类别:Biomedical and Life Sciences
  • 刊物主题:Life Sciences
    Biochemistry
    Animal Anatomy, Morphology and Histology
    Polymer Sciences
  • 出版者:Springer Netherlands
  • ISSN:1573-3904
文摘
Lactoferrin (LF) is a naturally occurring antimicrobial peptide that is cleaved by pepsin to lactoferricin (LFcin). LFcin has an enhanced antimicrobial activity as compared to that of LF. Recently several hetero- and homodimeric antimicrobial peptides stabilized by a single disulfide bond linking linear polypeptide chains have been discovered. We have demonstrated that the S–S bond heterodimerization of lipopeptide Laur-Orn-Orn-Cys–NH2 (peptide III) and the synthetic N-terminal peptide of human lactoferricin (peptide I) yields a dimer (peptide V), which is almost as microbiologically active as the more active monomer and at the same time it is much less toxic. Furthermore, it has been found that the S–S bond homodimerization of both peptide I and peptide III did not affect antimicrobial and haemolytic activity of the compounds. The homo- and heterodimerization of peptides I and III resulted in either reduction or loss of antifungal activity. This work suggests that heterodimerization of antimicrobial lipopeptides via intermolecular disulfide bond might be a powerful modification deserving consideration in the design of antimicrobial peptides.

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