Antimicrobial activities of heparin-binding peptides.

Forskningsoutput: TidskriftsbidragArtikel i vetenskaplig tidskrift

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.

Detaljer

Författare
Enheter & grupper
Forskningsområden

Ämnesklassifikation (UKÄ) – OBLIGATORISK

  • Infektionsmedicin
  • Dermatologi och venereologi

Nyckelord

Originalspråkengelska
Sidor (från-till)1219-1226
TidskriftEuropean Journal of Biochemistry
Volym271
Utgåva nummer6
StatusPublished - 2004
PublikationskategoriForskning
Peer review utfördJa

Nedladdningar

Ingen tillgänglig data

Relaterad forskningsoutput

Emma Nordahl, 2009, Department of Clinical Sciences, Lund University. 136 s.

Forskningsoutput: AvhandlingDoktorsavhandling (sammanläggning)

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