The self-assembly properties of peptide amphiphiles make them attractive for a range of applications, such as scaffolds for cell culture, drug delivery vehicles, or as stabilizing coatings for nanoparticles. The latter application requires derivatization of the amphiphiles to enable them to bind to, and interact with, a surface. This can be achieved by introduction of a thiol which facilitates binding to gold surfaces for example. However, small changes to the composition of peptide amphiphiles can have a large impact on their self-assembly behavior. Therefore, we have synthesized and characterized a range of amphiphiles with different peptide sequences, alkyl chain lengths, and with or without a terminal thiol. We have characterized their structure and self-assembly using circular dichroism (CD) spectroscopy, attenuated total reflection infrared (ATR-IR) spectroscopy, and transmission electron microscopy (TEM). We discuss how changes to the peptide sequence and alkyl chain affect self-assembly and compare the self-assembly properties of thiolated and non-thiolated amphiphiles. Such knowledge not only provides fundamental insights as to how self-assembly can be controlled, but will also be helpful in determining which amphiphiles are most suitable for use as stabilizing nanoparticle coatings.

中文翻译：

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硫醇化与非硫醇化肽两亲物的自组装

肽两亲物的自组装特性使其在一系列应用中具有吸引力，例如细胞培养支架、药物输送载体或作为纳米颗粒的稳定涂层。后一种应用需要两亲物的衍生化，使它们能够与表面结合并相互作用。这可以通过引入促进与例如金表面结合的硫醇来实现。然而，肽两亲物组成的微小变化会对它们的自组装行为产生很大的影响。因此，我们合成并表征了一系列具有不同肽序列、烷基链长度以及带有或不带有末端硫醇的两亲物。我们使用圆二色性 (CD) 光谱表征了它们的结构和自组装，衰减全反射红外 (ATR-IR) 光谱和透射电子显微镜 (TEM)。我们讨论了肽序列和烷基链的变化如何影响自组装，并比较了硫醇化和非硫醇化两亲物的自组装特性。这些知识不仅提供了关于如何控制自组装的基本见解，而且还将有助于确定哪些两亲物最适合用作稳定纳米粒子涂层。