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Interaction between tachyplesin I, an antimicrobial peptide derived from horseshoe crab, and lipopolysaccharide
Title: | Interaction between tachyplesin I, an antimicrobial peptide derived from horseshoe crab, and lipopolysaccharide |
Authors: | Kushibiki, Takahiro Browse this author | Kamiya, Masakatsu Browse this author | Aizawa, Tomoyasu Browse this author →KAKEN DB | Kumaki, Yasuhiro Browse this author | Kikukawa, Takashi Browse this author →KAKEN DB | Mizuguchi, Mineyuki Browse this author →KAKEN DB | Demura, Makoto Browse this author →KAKEN DB | Kawabata, Shun-ichiro Browse this author | Kawano, Keiichi Browse this author |
Keywords: | Antimicrobial peptide | Docking calculation | Lipopolysaccharide | NMR | Tachyplesin I |
Issue Date: | Mar-2014 |
Publisher: | Elsevier |
Journal Title: | Biochimica et Biophysica Acta : Proteins and Proteomics |
Volume: | 1844 |
Issue: | 3 |
Start Page: | 527 |
End Page: | 534 |
Publisher DOI: | 10.1016/j.bbapap.2013.12.017 |
PMID: | 24389234 |
Abstract: | 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 beta-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. (c) 2013 Elsevier B.V. All rights reserved. |
Type: | article (author version) |
URI: | http://hdl.handle.net/2115/56366 |
Appears in Collections: | 生命科学院・先端生命科学研究院 (Graduate School of Life Science / Faculty of Advanced Life Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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