Self-sorting is a spontaneous phenomenon that ensures the formation of complex yet ordered multicomponent systems and conceptualizes the design of artificial and orthogonally functional compartments. In the present study, we envisage chirality-mediated self-sorting in β-amyloid-inspired minimalistic peptide amphiphile (C₁₀-L/D-VFFAKK)-based nanofibers. The fidelity and stereoselectivity of chiral self-sorting was ascertained by Förster resonance energy transfer (FRET) by the judicious choice of a pyrene (Py)-hydroxy coumarin (HOCou) donor–acceptor pair tethered to the peptide sequences. Seed-promoted elongation of the homochiral peptide amphiphiles investigated by AFM image analyses and Thioflavin-T (ThT) binding study further validated the chiral recognition of the L/D peptide nanofibers. Moreover, direct visualization of the chirality-driven self-sorted nanofibers is reported using super-resolution microscopy that exhibits enantioselective enzymatic degradation for L-peptide fibers. Such enantioselective weakening of the hydrogels may be used for designing stimuli-responsive orthogonal compartments for delivery applications.

中文翻译：

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淀粉样物质启发的简约肽两亲物中的酶响应手性自分选。

自分类是一种自发现象，可确保形成复杂而有序的多组分系统，并概念化了人造和正交功能隔室的设计。在本研究中，我们设想了由β-淀粉样蛋白启发的简约肽两亲物（C ₁₀ - L / D-VFFAKK）纳米纤维。手性自分选的保真度和立体选择性是通过Förster共振能量转移（FRET）来确定的，方法是明智地选择拴在肽序列上的pyr（Py）-羟基香豆素（HOCou）供体-受体对。通过原子力显微镜图像分析和硫黄素-T（ThT）结合研究研究的同手性肽两亲物的种子促进的伸长进一步验证了L / D肽纳米纤维的手性识别。此外，使用超分辨率显微镜报道了手性驱动的自选纳米纤维的直接可视化，该显微镜显示了对映体对L的对映选择性酶促降解肽纤维。水凝胶的这种对映选择性减弱可用于设计用于递送应用的刺激响应正交隔室。