Structure of the antimicrobial peptide tachystatin A

Naoki Fujitani, Shun Ichiro Kawabata, Tsukasa Osaki, Yasuhiro Kumaki, Makoto Demura, Katsutoshi Nitta, Keiichi Kawano

研究成果: ジャーナルへの寄稿学術誌査読

41 被引用数 (Scopus)


The solution structure of antimicrobial peptide tachystatin A from the Japanese horseshoe crab (Tachypleus tridentatus) was determined by two-dimensional nuclear magnetic resonance measurements and distance-restrained simulated annealing calculations. The correct pairs of disulfide bonds were also confirmed in this study. The obtained structure has a cysteine-stabilized triple-stranded β-sheet as a dominant secondary structure and shows an amphiphilic folding observed in many membrane-interactive peptides. Interestingly, tachystatin A shares structural similarities with the calcium channel antagonist ω-agatoxin IVA isolated from spider toxin and mammalian defensins, and we predicted that ω-agatoxin IVA also have the antifungal activity. These structural comparisons and functional correspondences suggest that tachystatin A and ω-agatoxin IVA may exert the antimicrobial activity in a manner similar to defensins, and we have confirmed such activity using fungal culture assays. Furthermore, tachystatin A is a chitin-binding peptide, and ω-agatoxin IVA also showed chitin-binding activities in this study. Tachystatin A and ω-agatoxin IVA showed no structural homology with well known chitin-binding motifs, suggesting that their structures belong to a novel family of chitin-binding peptides. Comparison of their structures with those of cellulose-binding proteins indicated that Phe9 of tachystatin A might be an essential residue for binding to chitin.

ジャーナルJournal of Biological Chemistry
出版ステータス出版済み - 6月 28 2002

!!!All Science Journal Classification (ASJC) codes

  • 生化学
  • 分子生物学
  • 細胞生物学


「Structure of the antimicrobial peptide tachystatin A」の研究トピックを掘り下げます。これらがまとまってユニークなフィンガープリントを構成します。