The two-dimensional (2D) homogeneous assembly of nanoparticle monolayer arrays onto a broad range of substrates constitutes an important challenge for chemistry, nanotechnology, and material science. α-Synuclein (αS) is an intrinsically disordered protein associated with neuronal protein complexes and has a high degree of structural plasticity and chaperone activity. The C-terminal domain of αS has been linked to the noncovalent interactions of this protein with biological targets and the activity of αS in presynaptic connections. Herein, we have systematically studied peptide fragments of the chaperone-active C-terminal sequence of αS and identified a 17-residue peptide that preserves the versatile binding nature of αS. Attachment of this short peptide to gold nanoparticles afforded colloidally stable nanoparticle suspensions that allowed the homogeneous 2D adhesion of the conjugates onto a wide variety of surfaces, including the formation of crystalline nanoparticle superlattices. The peptide sequence and the strategy reported here describe a new adhesive molecule for the controlled monolayer adhesion of metal nanoparticles and sets a stepping-stone toward the potential application of the adhesive properties of αS.

中文翻译：

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来自α-突触核蛋白的C末端域的粘附肽，用于纳米粒子在基底上的单层吸附

纳米粒子单层阵列在各种基材上的二维（2D）均匀组装构成了化学，纳米技术和材料科学的重要挑战。α-突触核蛋白（αS）是与神经元蛋白复合物相关的一种内在失调的蛋白，具有高度的结构可塑性和分子伴侣活性。αS的C末端结构域已与该蛋白质与生物学靶标的非共价相互作用以及突触前连接中αS的活性相关。在本文中，我们系统地研究了αS的伴侣活性C端序列的肽片段，并鉴定了保留了αS通用结合性质的17个残基的肽。将该短肽附着到金纳米颗粒上可得到胶体稳定的纳米颗粒悬浮液，该悬浮液可使结合物均匀2D粘附在各种表面上，包括形成晶体纳米颗粒超晶格。此处报道的肽序列和策略描述了一种用于控制金属纳米颗粒单层粘附的新型粘附分子，并为αS粘附特性的潜在应用奠定了基础。