Cysteine-stabilized αβ defensins: From a common fold to antibacterial activity

@article{Dias2015CysteinestabilizedD,
  title={Cysteine-stabilized $\alpha$$\beta$ defensins: From a common fold to antibacterial activity},
  author={Renata de Oliveira Dias and Oct{\'a}vio Luiz Franco},
  journal={Peptides},
  year={2015},
  volume={72},
  pages={64-72}
}
Antimicrobial peptides (AMPs) seem to be promising alternatives to common antibiotics, which are facing increasing bacterial resistance. Among them are the cysteine-stabilized αβ defensins. These peptides are small, with a length ranging from 34 to 54 amino acid residues, cysteine-rich and extremely stable, normally composed of an α-helix and three β-strands stabilized by three or four disulfide bonds and commonly found in several organisms. Moreover, animal and plant CSαβ defensins present… Expand
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