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

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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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