Interaction between tachyplesin I, an antimicrobial peptide derived from horseshoe crab, and lipopolysaccharide
Interaction between tachyplesin I, an antimicrobial peptide derived from horseshoe crab, and lipopolysaccharide
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DOI：
10.1016/j.bbapap.2013.12.017
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发表时间：
2014-03-01
影响因子：
3.2
通讯作者：
Kawano, Keiichi
中科院分区：
文献类型：
--
作者：
Kushibiki, Takahiro;Kamiya, Masakatsu;Kawano, Keiichi
脂多糖（LPS）是革兰氏阴性菌外膜的主要成分，是抗菌肽（AMP）的第一个相互作用位点。为了更好地了解LPS和AMP之间的相互作用，我们测定了鲎抗菌肽鲎素I（tachyplesin I，TP I）与LPS结合状态下的结构，并利用对接程序提出了TP I与LPS的复合物结构。CD和NMR测量显示，与LPS结合略微延长了TP I的两条β链，并稳定了TP I的整个结构。TP I的固有色氨酸的荧光波长和在存在或不存在LPS的情况下的荧光猝灭表明色氨酸残基被掺入LPS的疏水环境中。最后，我们成功地提出了一个结构模型的复合物的TP I和LPS通过使用对接程序。计算的模型结构表明，TP I的阳离子残基与磷酸基团和LPS的羧基相互作用，而疏水残基与LPS的酰基链相互作用。(c)2013 Elsevier B.V.保留所有权利。
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.