Antimicrobial activities of heparin-binding peptides.
(2004) In European Journal of Biochemistry 271(6). p.1219-1226- Abstract
- 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... (More)
- 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. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/121424
- author
- Andersson, Emma ; Rydengård, Victoria LU ; Sonesson, Andreas LU ; Mörgelin, Matthias LU ; Björck, Lars LU and Schmidtchen, Artur LU
- organization
- publishing date
- 2004
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- heparin binding, defensin, antimicrobial, cathelicidin, glycosaminoglycan
- in
- European Journal of Biochemistry
- volume
- 271
- issue
- 6
- pages
- 1219 - 1226
- publisher
- Wiley-Blackwell
- external identifiers
-
- wos:000220006500016
- pmid:15009200
- scopus:1642281222
- ISSN
- 0014-2956
- DOI
- 10.1111/j.1432-1033.2004.04035.x
- language
- English
- LU publication?
- yes
- id
- 01b74850-44fd-450e-bff8-cb120ab89be6 (old id 121424)
- date added to LUP
- 2016-04-01 16:19:13
- date last changed
- 2022-02-20 05:17:38
@article{01b74850-44fd-450e-bff8-cb120ab89be6,
abstract = {{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.}},
author = {{Andersson, Emma and Rydengård, Victoria and Sonesson, Andreas and Mörgelin, Matthias and Björck, Lars and Schmidtchen, Artur}},
issn = {{0014-2956}},
keywords = {{heparin
binding; defensin; antimicrobial; cathelicidin; glycosaminoglycan}},
language = {{eng}},
number = {{6}},
pages = {{1219--1226}},
publisher = {{Wiley-Blackwell}},
series = {{European Journal of Biochemistry}},
title = {{Antimicrobial activities of heparin-binding peptides.}},
url = {{https://lup.lub.lu.se/search/files/4636491/623976.pdf}},
doi = {{10.1111/j.1432-1033.2004.04035.x}},
volume = {{271}},
year = {{2004}},
}