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Lipid membrane interactions of self-assembling antimicrobial nanofibers: effect of PEGylation

机译：自组装抗微生物纳米纤维的脂质膜相互作用：聚乙二醇化的作用

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摘要

Supramolecular assembly and PEGylation (attachment of a polyethylene glycol polymer chain) of peptides can be an effective strategy to develop antimicrobial peptides with increased stability, antimicrobial efficacy and hemocompatibility. However, how the self-assembly properties and PEGylation affect their lipid membrane interaction is still an unanswered question. In this work, we use state-of-the-art small angle X-ray and neutron scattering (SAXS/SANS) together with neutron reflectometry (NR) to study the membrane interaction of a series of multidomain peptides, with and without PEGylation, known to self-assemble into nanofibers. Our approach allows us to study both how the structure of the peptide and the membrane are affected by the peptide-lipid interactions. When comparing self-assembled peptides with monomeric peptides that are not able to undergo assembly due to shorter chain length, we found that the nanofibers interact more strongly with the membrane. They were found to insert into the core of the membrane as well as to absorb as intact fibres on the surface. Based on the presented results, PEGylation of the multidomain peptides leads to a slight net decrease in the membrane interaction, while the distribution of the peptide at the interface is similar to the non-PEGylated peptides. Based on the structural information, we showed that nanofibers were partially disrupted upon interaction with phospholipid membranes. This is in contrast with the considerable physical stability of the peptide in solution, which is desirable for an extendedin vivocirculation time.
机译：肽的超分子组装和PEG化（聚乙二醇聚合物链的附着）可以是开发抗微生物肽的有效策略，以增加稳定性，抗微生物功效和血液相位性。然而，自组装性质和聚乙二醇化如何影响其脂质膜相互作用仍然是一个未答复的问题。在这项工作中，我们使用最先进的小角度X射线和中子散射（SAXS / SAN）以及中子反射率（NR），以研究一系列多源肽的膜相互作用，有和没有聚乙二醇化，已知自我组装成纳米纤维。我们的方法使我们能够研究肽和膜的结构如何受肽 - 脂质相互作用的影响。当比较具有由于较短的链长而不能经历组件的单体肽的自组装肽，我们发现纳米纤维与膜更强烈地相互作用。发现它们插入膜的核心，并在表面上吸收完整的纤维。基于所呈现的结果，多畴肽的聚乙二醇化导致膜相互作用的轻微净减少，而肽在界面处的分布类似于非聚乙二醇化肽。基于结构信息，我们表明纳米纤维在与磷脂膜的相互作用时部分破坏。这与溶液中肽的相当大的物理稳定性相反，这对于延长素的vivocirculation时间是期望的。

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  • 来源
    《RSC Advances》 |2020年第58期|共12页
  • 作者

    Nielsen Josefine Eilso; Koenig Nico; Yang Su; Skoda Maximilian W. A.; Maestro Armando; Dong He; Cardenas Marite; Lund Reidar;

  • 作者单位

    Univ Oslo Dept Chem N-0315 Oslo Norway;

    Univ Oslo Dept Chem N-0315 Oslo Norway;

    Univ Texas Arlington Dept Chem &

    Biochem Arlington TX 76019 USA;

    Rutherford Appleton Lab Sci &

    Technol Facil Council ISIS Pulsed Neutron &

    Muon Source Harwell Sci &

    Innovat Campus Didco OX11 0QX Oxon England;

    Inst Laue Langevin F-38000 Grenoble France;

    Univ Texas Arlington Dept Chem &

    Biochem Arlington TX 76019 USA;

    Malmo Univ Biofilms Res Ctr Biointerfaces Dept Biomed Sci Hlth &

    Soc S-20506 Malmo Sweden;

    Univ Oslo Dept Chem N-0315 Oslo Norway;

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  • 正文语种 eng
  • 中图分类 化学;
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