Goldilocks Energy Minimum: Peptide-Based Reversible Aggregation and Biosensing.
Goldilocks Energy Minimum: Peptide-Based Reversible Aggregation and Biosensing.
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金发姑娘能量最低：基于肽的可逆聚集和生物传感。
DOI：
10.1021/acsami.3c09627
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发表时间：
2023
影响因子：
9.5
通讯作者：
Jokerst,JesseV
中科院分区：
文献类型：
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作者：
Yim,Wonjun;Retout,Maurice;Chen,AmandaA;Ling,Chuxuan;Amer,Lubna;Jin,Zhicheng;Chang,Yu-Ci;Chavez,Saul;Barrios,Karen;Lam,Benjamin;Li,Zhi;Zhou,Jiajing;Shi,Lingyan;Pascal,TodA;Jokerst,JesseV
基于金纳米颗粒（AuNP）聚集的比色生物传感器通常受到生物流体中的基质干扰、差的特异性和临床样品的有限实用性的挑战。在这里，我们提出了一种肽驱动的纳米级拆解方法，其中静电吸引诱导的AuNP聚集体响应于蛋白水解切割而解离。最初，柠檬酸盐包被的金纳米粒子组装通过一个短的阳离子肽（RRK）和其特征在于实验和模拟。然后使用解离肽可逆地解离作为靶蛋白酶检测的函数的AuNP聚集体，即，主要蛋白酶（Mpro），严重急性呼吸综合征冠状病毒2的生物标志物。解离倾向取决于肽长度、亲水性、电荷和配体结构。最后，我们的解离策略通过Mprocleavage提供了快速和独特的光学信号，在唾液中的检测限为12.3 nM。我们的解离肽有效地解离不同基质中的等离子体组装体，包括100%人唾液、尿液、血浆和海水，以及其他类型的等离子体纳米颗粒，如银。我们的肽使能解离平台提供了一种简单、基质不敏感且通用的蛋白酶传感方法。
Colorimetric biosensors based on gold nanoparticle (AuNP) aggregation are often challenged by matrix interference in biofluids, poor specificity, and limited utility with clinical samples. Here, we propose a peptide-driven nanoscale disassembly approach, where AuNP aggregates induced by electrostatic attractions are dissociated in response to proteolytic cleavage. Initially, citrate-coated AuNPs were assembled via a short cationic peptide (RRK) and characterized by experiments and simulations. The dissociation peptides were then used to reversibly dissociate the AuNP aggregates as a function of target protease detection, i.e., main protease (Mpro), a biomarker for severe acute respiratory syndrome coronavirus 2. The dissociation propensity depends on peptide length, hydrophilicity, charge, and ligand architecture. Finally, our dissociation strategy provides a rapid and distinct optical signal through Mprocleavage with a detection limit of 12.3 nM in saliva. Our dissociation peptide effectively dissociates plasmonic assemblies in diverse matrices including 100% human saliva, urine, plasma, and seawater, as well as other types of plasmonic nanoparticles such as silver. Our peptide-enabled dissociation platform provides a simple, matrix-insensitive, and versatile method for protease sensing.