Fibrillar structures formed by covalently bound, short, β-stranded peptides on self-assembled monolayers.
Fibrillar structures formed by covalently bound, short, β-stranded peptides on self-assembled monolayers.
复制标题
由共价结合的短 β 链肽在自组装单层上形成的纤维状结构。
作者：
Jason W Dugger;Lauren J. Webb
在无机基质上维持或复制生物分子结构的能力有可能影响传感和分子电子学等不同领域，以及生物自组装和结构功能关系的研究。由于生物分子的结构和自组装对其局部化学和静电环境极其敏感，因此在非生物环境（包括表面）中复制或模仿生物功能的目标具有挑战性。然而，对制备的表面进行简单且良好表征的化学修饰可用于调节无机材料的表面化学、结构、静电和反应性，以促进生物功能化和功能。在这里，我们描述了通过 Huisgen 环加成或“点击”反应将含有炔基的 13 个残基 β-链肽共价连接到用叠氮化物封端的自组装单层功能化的平坦金表面。使用 X 射线光电子能谱、掠入射角反射吸收红外光谱、表面圆二色性和原子力显微镜对这些表面的化学成分和结构形貌进行了表征。表面结合的 β 链自组装成反平行 β 片层，在反应表面形成直径为 24.9 ± 1.6 nm、高度为 2.83 ± 0.74 nm 的纤维结构。本文的结果提供了一个平台，用于研究和控制生物分子自组装成更大的超分子结构的过程，同时允许通过表面的化学功能化进行可调控制。对纤维结构形成机制的兴趣通常与神经退行性疾病有关，例如阿尔茨海默氏症和帕金森氏症，但纤维实际上可能代表了一类更大类别的肽和蛋白质的热力学低能构象。这里开发的协议是重要的一步，不仅揭示了决定自组装的因素，而且揭示了这种纤维状上层结构形成的机制。
The ability to maintain or reproduce biomolecular structures on inorganic substrates has the potential to impact diverse fields such as sensing and molecular electronics, as well as the study of biological self-assembly and structure-function relationships. Because the structure and self-assembly of biomolecules are exquisitely sensitive to their local chemical and electrostatic environment, the goal of reproducing or mimicking biological function in an abiological environment, including at a surface, is challenging. However, simple and well-characterized chemical modifications of prepared surfaces can be used to tune surface chemistry, structure, electrostatics, and reactivity of inorganic materials to facilitate biofunctionalization and function. Here, we describe the covalent attachment of 13-residue β-stranded peptides containing alkyne groups to a flat gold surface functionalized with an azide-terminated self-assembled monolayer through a Huisgen cycloaddition, or "click", reaction. The chemical composition and structural morphology of these surfaces were characterized using X-ray photoelectron spectroscopy, grazing incidence angle reflection-absorption infrared spectroscopy, surface circular dichroism, and atomic force microscopy. The surface-bound β-strands self-assemble into antiparallel β-sheets to form fibrillar structures 24.9 ± 1.6 nm in diameter and 2.83 ± 0.74 nm in height on the reactive surface. The results herein provide a platform for studying and controlling the self-assembly process of biomolecules into larger supermolecular structures while allowing tunable control through chemical functionalization of the surface. Interest in the mechanisms of formation of fibrillar structures has most commonly been associated with neurodegenerative diseases, such as Alzheimer's and Parkinson's, but fibrils may actually represent the thermodynamic low-energy conformation of a much larger class of peptides and proteins. The protocol developed here is an important step toward uncovering not only the factors that dictate self-assembly but also the mechanisms by which this fibrillar class of superstructures forms.
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