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

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...

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Bibliographic Details
Published in:Biochimica et biophysica acta 2014-03, Vol.1844 (3), p.527-534
Main Authors: Kushibiki, Takahiro, Kamiya, Masakatsu, Aizawa, Tomoyasu, Kumaki, Yasuhiro, Kikukawa, Takashi, Mizuguchi, Mineyuki, Demura, Makoto, Kawabata, Shun-ichiro, Kawano, Keiichi
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Anti-Infective Agents - chemistry
Antimicrobial Cationic Peptides - chemistry
Antimicrobial peptide
Circular Dichroism
Decapoda
DNA-Binding Proteins - chemistry
Docking calculation
Horseshoe Crabs
Lipopolysaccharide
Lipopolysaccharides - chemistry
Models, Molecular
Molecular Sequence Data
NMR
Nuclear Magnetic Resonance, Biomolecular
Peptides, Cyclic - chemistry
Spectrometry, Fluorescence
Tachyplesin I
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Summary: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. •The structure of TP I in LPS micelles was determined by NMR.•The TP I–LPS complex model was proposed by docking calculation.•The N and C terminal residues of TP I were involved in binding to LPS.
ISSN:1570-9639
0006-3002
1878-1454
DOI:10.1016/j.bbapap.2013.12.017