Interaction between tachyplesin I, an antimicrobial peptide derived from horseshoe crab, and lipopolysaccharide

Takahiro Kushibiki, Masakatsu Kamiya, Tomoyasu Aizawa, Yasuhiro Kumaki, Takashi Kikukawa, Mineyuki Mizuguchi, Makoto Demura, Shun Ichiro Kawabata, Keiichi Kawano

研究成果: Contribution to journalArticle査読

49 被引用数 (Scopus)

抄録

Lipopolysaccharide (LPS) is a major constituent of the outer membrane of Gram-negative bacteria and is the very first site of interactions with antimicrobial peptides (AMPs). In order to gain better insight into the interaction between LPS and AMPs, we determined the structure of tachyplesin I (TP I), an antimicrobial peptide derived from horseshoe crab, in its bound state with LPS and proposed the complex structure of TP I and LPS using a docking program. CD and NMR measurements revealed that binding to LPS slightly extends the two β-strands of TP I and stabilizes the whole structure of TP I. The fluorescence wavelength of an intrinsic tryptophan of TP I and fluorescence quenching in the presence or absence of LPS indicated that a tryptophan residue is incorporated into the hydrophobic environment of LPS. Finally, we succeeded in proposing a structural model for the complex of TP I and LPS by using a docking program. The calculated model structure suggested that the cationic residues of TP I interact with phosphate groups and saccharides of LPS, whereas hydrophobic residues interact with the acyl chains of LPS.

本文言語英語
ページ(範囲)527-534
ページ数8
ジャーナルBiochimica et Biophysica Acta - Proteins and Proteomics
1844
3
DOI
出版ステータス出版済み - 3 2014

All Science Journal Classification (ASJC) codes

  • 分析化学
  • 生物理学
  • 生化学
  • 分子生物学

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