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与细菌膜靶向机制相关的阿尼辛-1 的特征区域。

The characteristic region of arenicin-1 involved with a bacterial membrane targeting mechanism.

机构信息

School of Life Sciences and Biotechnology, College of Natural Sciences, Kyungpook National University, 1370 Sankyuk-dong, Puk-ku, Daegu 702-701, Republic of Korea.

出版信息

Biochem Biophys Res Commun. 2011 Feb 18;405(3):422-7. doi: 10.1016/j.bbrc.2011.01.046. Epub 2011 Jan 15.

Abstract

The antimicrobial peptide arenicin-1 consists of two antiparallel β-sheets linked by a hydrophilic β-turn. To determine the role of a specific region found in a particular β-sheet structure of the peptide for antibacterial activity, two analogs with N-terminal deletions (RW) and substitutions of Arg to Ala in the β-turn region were designed. In the minimum inhibitory concentration (MIC) test, the antibacterial activities of the analogs were reduced for both Gram-positive and Gram-negative bacteria, when compared to arenicin-1. The influence of the decrease in hydrophobicity on the antibacterial activity was confirmed by a hemolytic assay. Through flow cytometric analysis using propidium iodide (PI) and a 1,6-diphenyl-1,3,5-hexatriene (DPH) assay, it was confirmed that the analogs decreased the degree of plasma membrane permeability compared to arenicin-1. In particular, analog 2 showed a lower permeability in Gram-negative bacteria than in Gram-positive bacteria. The results indicate that a reduction in the net charge weakened the electrostatic interactions between the peptides and the negatively charged membranes. In liposomes, which mimic bacterial membranes, due to a reduced binding affinity to the membranes, the analogs could not deeply penetrate into the hydrocarbon region and induce enough fluorescein isothiocyanate-dextran (FD) leakage compared to that of arenicin-1. It is thought that the Arg residue in the hydrophilic β-turn region is more important to antibacterial activity than the Arg residue in the N-terminal region. This study suggests that the Arg and Trp residues in the N-terminal region and the Arg residue in the β-turn region of arenicin-1 play a key role in antibacterial activity.

摘要

抗菌肽 arenicin-1 由两个反平行的β-折叠通过一个亲水的β-转角连接而成。为了确定在肽的特定β-折叠结构中发现的特定区域对于抗菌活性的作用,设计了两种具有 N 端缺失(RW)和β-转角区域中精氨酸取代为丙氨酸的类似物。在最低抑菌浓度(MIC)测试中,与 arenicin-1 相比,类似物对革兰氏阳性菌和革兰氏阴性菌的抗菌活性均降低。通过溶血试验证实了疏水性降低对抗菌活性的影响。通过使用碘化丙啶(PI)和 1,6-二苯基-1,3,5-己三烯(DPH)测定法进行流式细胞术分析,证实类似物与 arenicin-1 相比降低了质膜通透性的程度。特别是,类似物 2 在革兰氏阴性菌中的通透性低于革兰氏阳性菌。结果表明,净电荷的减少削弱了肽与带负电荷的膜之间的静电相互作用。在模拟细菌膜的脂质体中,由于与膜的结合亲和力降低,类似物不能像 arenicin-1 那样深入渗透到烃区域并诱导足够的荧光素异硫氰酸酯-葡聚糖(FD)渗漏。据认为,亲水β-转角区域中的精氨酸残基比 N-末端区域中的精氨酸残基对抗菌活性更为重要。这项研究表明,arenicin-1 的 N-末端区域中的 Arg 和 Trp 残基以及β-转角区域中的 Arg 残基在抗菌活性中起着关键作用。

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