Antimicrobial activities of heparin-binding peptides.
Author
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.
Publishing year
2004
Language
English
Pages
1219-1226
Publication/Series
European Journal of Biochemistry
Volume
271
Issue
6
Full text
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Document type
Journal article
Publisher
Wiley-Blackwell
Topic
- Infectious Medicine
- Dermatology and Venereal Diseases
Keywords
- heparin binding
- defensin
- antimicrobial
- cathelicidin
- glycosaminoglycan
Status
Published
ISBN/ISSN/Other
- ISSN: 0014-2956