Structure-activity relation of human beta-defensin 3: influence of disulfide bonds and cysteine substitution on antimicrobial activity and cytotoxicity.

  title={Structure-activity relation of human beta-defensin 3: influence of disulfide bonds and cysteine substitution on antimicrobial activity and cytotoxicity.},
  author={Enno Kl{\"u}ver and Sandra Schulz-Maronde and Svenja Scheid and Bernd Meyer and Wolf Georg Forssmann and Knut Adermann},
  volume={44 28},
Human beta-defensins form a group of cysteine-rich antimicrobial peptides which have been found in epithelial tissue and, more recently, in the male genital tract. They play a role in the defense against microbial pathogens in innate immunity and display additional chemotactic functions in the adaptive immune system. An important characteristic of antimicrobial peptides is that they also exhibit toxic potential on eukaryotic cells. Very little is known about the structure dependence of… Expand
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Membrane disruptive antimicrobial activities of human β-defensin-3 analogs.
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Antibacterial activities of synthetic peptides corresponding to the carboxy-terminal region of human β-defensins 1–3
Peptides spanning the carboxy-terminal region of human beta- defensins could be of help in understanding facets of antimicrobial activity of beta-defensins such as salt sensitivity and mechanisms of bacterial membrane damage. Expand
Structure–activity relationship of human liver-expressed antimicrobial peptide 2
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