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首页> 外文期刊>International Journal of Biological Macromolecules: Structure, Function and Interactions >Charges' interaction in polyelectrolyte (nano)complexing of His(6)-OPH with peptides: Unpredictable results due to imperfect or useless concept?
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Charges' interaction in polyelectrolyte (nano)complexing of His(6)-OPH with peptides: Unpredictable results due to imperfect or useless concept?

机译：对其（6） - 酚肽的聚电解质（纳米）络合中的电力相互作用：由于不完美或无用的概念而导致的结果不可预测结果？

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摘要

Quorum Quenching (QQ) enzymes can be used to prevent bacterial antibiotic resistance by degradation of Quorum Sensing (QS) signaling molecules, for example N-acyl homoserine lactones (AHLs). This paper is aimed at the in silico investigation of the possible combinations of hexahistidine-tagged organophosphorus hydrolase (His(6)-OPH) with antimicrobial peptides (AMPs) to improve the enzyme activity and, promisingly, stability. This shall help creating a nanosized QQ preparation capable to hydrolyze different AHLs and possessing an antimicrobial activity. To achieve this, binding of AMPs and His(6)-OPH was simulated by molecular docking, and various interaction parameters (affinity, charge, contact area, etc.) of the generated models were studied. Both anionic and cationic polypeptides were shown to bind to His(6)-OPH with negligible effect of their charge, that significantly deviates from the charge-to-charge interaction concept. The (nano)complexes of His(6)-OPH with Indolicidin and Temporin A appear to have the most balanced characteristics which were issued experimentally also. (C) 2019 Elsevier B.V. All rights reserved.
机译：可以使用仲裁猝灭（QQ）酶来防止仲裁感测（QS）信号分子的降解细菌抗生素抗性，例如N-酰基均静脉内酯（AHL）。本文旨在硅藻研究六三羟胺标记的有机磷水解酶（他（6） - 粒子）与抗微生物肽（AMP）的组合，以改善酶活性，并承诺，稳定性。这应有助于产生纳米QQ制剂，能够水解不同的AHL并具有抗微生物活性。为了实现这一点，通过分子对接模拟了AMP和他的（6）孔的结合，以及所产生模型的各种相互作用参数（亲和力，电荷，接触面积等）。显示阴离子和阳离子多肽均被显示为与他（6）倍孔的效果结合，其电荷效果可忽略不计，这显着偏离了充电与电荷相互作用概念。他（6） - 蛋白与吲哚嗪和颞蛋白A的复合物似乎具有实验发布的最平衡的特征。 （c）2019 Elsevier B.v.保留所有权利。

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