Role of amino acid residues within the disulfide loop of thanatin, a potent antibiotic peptide.

@article{Lee2002RoleOA,
  title={Role of amino acid residues within the disulfide loop of thanatin, a potent antibiotic peptide.},
  author={Myung Kyu Lee and Lina Cha and Si Hyung Lee and Kyung-soo Hahm},
  journal={Journal of biochemistry and molecular biology},
  year={2002},
  volume={35 3},
  pages={291-6}
}
Thanatin, a 21-residue peptide, is an inducible insect peptide with a broad range of activity against bacteria and fungi. It has a C-terminal disulfide loop, like the frog skin secretion antimicrobial peptides of the brevinin family. In this study, we tried to find the effect of a number of amino acids between the disulfide bond. Thanatin showed stronger antibacterial activity to Gram negative bacteria than other mutants, except Th1; whereas, the mutant peptides with deletion had higher… CONTINUE READING