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

@article{Klver2005StructureactivityRO,
  title={Structure-activity relation of human beta-defensin 3: influence of disulfide bonds and cysteine substitution on antimicrobial activity and cytotoxicity.},
  author={E. Kl{\"u}ver and S. Schulz-Maronde and S. Scheid and B. Meyer and W. Forssmann and K. Adermann},
  journal={Biochemistry},
  year={2005},
  volume={44 28},
  pages={
          9804-16
        }
}
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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