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Antimicrobial activities of heparin-binding peptides.

In English

Författare

Summary, in English

Antimicrobial peptides are effector molecules of the innate immune system. We recently showed that the human antimicrobial peptides alpha-defensin and LL-37 bind to glycosaminoglycans (heparin and dermatan sulphate). Here we demonstrate the obverse, i.e. structural motifs associated with heparin affinity (cationicity, amphipaticity, and consensus regions) may confer antimicrobial properties to a given peptide. Thus, heparin-binding peptides derived from laminin isoforms, von Willebrand factor, vitronectin, protein C inhibitor, and fibronectin, exerted antimicrobial activities against Gram-positive and Gram-negative bacteria. Similar results were obtained using heparin-binding peptides derived from complement factor C3 as well as consensus sequences for heparin-binding (Cardin and Weintraub motifs). These sequence motifs, and additional peptides, also killed the fungus Candida albicans. These data will have implications for the search for novel antimicrobial peptides and utilization of heparin-protein interactions should be helpful in the identification and purification of novel antimicrobial peptides from complex biological mixtures. Finally, consensus regions may serve as templates for de novo synthesis of novel antimicrobial molecules.

Publiceringsår

2004

Språk

Engelska

Sidor

1219-1226

Publikation/Tidskrift/Serie

European Journal of Biochemistry

Volym

271

Issue

6

Dokumenttyp

Artikel i tidskrift

Förlag

Wiley-Blackwell

Ämne

  • Infectious Medicine
  • Dermatology and Venereal Diseases

Nyckelord

  • heparin binding
  • defensin
  • antimicrobial
  • cathelicidin
  • glycosaminoglycan

Status

Published

ISBN/ISSN/Övrigt

  • ISSN: 0014-2956