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首页> 外文期刊>The FEBS journal >Antibacterial action of synthetic antilipopolysaccharide peptides (SALP) involves neutralization of both membrane-bound and free toxins
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Antibacterial action of synthetic antilipopolysaccharide peptides (SALP) involves neutralization of both membrane-bound and free toxins

机译：合成抗胆糖肽（SALP）的抗菌作用涉及中和两种膜结合和自由毒素

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Increasing failure of conventional antibiotics to combat bacterial infections requires the urgent development of new antibacterial drugs; a promising class of new drugs based on antimicrobial peptides. Here, we studied the molecular interaction of polycationic synthetic antilipopolysaccharide peptides (SALPs) with various gram-negative and gram-positive bacteria, including resistant strains. The analysis of antimicrobial activity by conventional techniques and atomic force microscopy showed a strict dependence on amino acid (aa) sequences, with the type of amino acid, its position within the primary structure, and the sequence length being critical parameters. By monitoring lipopolysaccharide (LPS)- or bacteria-induced cytokine production in human mononuclear cells and whole blood, we found a direct link between the binding of the lead compound Pep19-2.5 to Salmonella enterica and the anti-inflammatory activity of the peptide. Thermodynamic analysis of Pep19-2.5 binding to the bacterial cell envelope showed an exothermic reaction with saturation characteristics, whereas small-angle X-ray scattering data indicated a direct attachment of Pep19-2.5 to the bacterial cell envelope. This binding preferentially takes place to the LPS outer monolayer, as evidenced by the change in the LPS acyl chain and phosphate vibrational bands seen by Fourier-transform infrared spectroscopy. We report here that the anti-inflammatory activity of Pep19-2.5 is not only connected with neutralization of cell-free bacterial toxins but also with a direct binding of the peptide to the outer leaflet of the bacterial outer membrane.
机译：常规抗生素的失效不断打击细菌感染需要迫切地发展新的抗菌药物;基于抗微生物肽的新药物阶级的一类。在此，我们研究了各种革兰氏阴性和革兰氏阳性细菌的聚阳离子合成抗胆糖肽（SALP）的分子相互作用，包括抗性菌株。通过常规技术和原子力显微镜分析抗微生物活性的分析显示，对氨基酸（AA）序列的严格依赖性，氨基酸的类型，其在初级结构内的位置，并且序列长度是关键参数。通过监测人单核细胞和全血中的脂多糖（LPS） - 或细菌诱导的细胞因子产生，我们发现铅化合物PEP19-2.5与沙门氏菌的结合与肽的抗炎活性之间的直接联系。 Pep19-2.5的热力学分析与细菌细胞包膜的结合显示出与饱和特性的放热反应，而小角度X射线散射数据表明PeP19-2.5的直接附着到细菌细胞包络。该结合优先发生在LPS外部单层，如傅立叶变换红外光谱观察到的LPS酰基链和磷酸振动带中的变化所证明的。我们在此报告Pep19-2.5的抗炎活性不仅与无细菌细菌毒素的中和相连，而且与肽的直接结合到细菌外膜的外叶片。

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