Solution and micelle-bound structures of tachyplesin I and its active aromatic linear derivatives.

@article{Laederach2002SolutionAM,
  title={Solution and micelle-bound structures of tachyplesin I and its active aromatic linear derivatives.},
  author={Alain Laederach and Amy H. Andreotti and D. Bruce Fulton},
  journal={Biochemistry},
  year={2002},
  volume={41 41},
  pages={
          12359-68
        }
}
Tachyplesin I is a 17-residue peptide isolated from the horseshoe crab, Tachypleus tridentatus. It has high antimicrobial activity and adopts a beta-hairpin conformation in solution stabilized by two cross-strand disulfide bonds. We report an NMR structural investigation of wild-type tachyplesin I and three linear derivatives (denoted TPY4, TPF4, and TPA4 in which the bridging cysteine residues are uniformly replaced with tyrosine, phenylalanine, and alanine, respectively). The three… CONTINUE READING
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