Zhou Juan, Gao Cai, Ding Yanru, Nie Zhenlin, Xu Mu, Fu Peiwen, He Bangshun, Wang Shukui, Xia Xing-Hua, Wang Kang
Department of Laboratory Medicine, Nanjing First Hospital, Nanjing Medical University, Nanjing 210006, China.
State Key Laboratory of Analytical Chemistry for Life Science, School of Chemistry and Chemical Engineering, Nanjing University, Nanjing 210023, China.
Nano Lett. 2025 Apr 16;25(15):6325-6331. doi: 10.1021/acs.nanolett.5c01214. Epub 2025 Apr 3.
Direct detection of proteins, especially their conformation and configuration information, at the single molecule level, is challenging in various biotechnological fields. Plasmonic nanopores have raised attention as multidimensional biosensors with single molecule (SM) sensitivity. Here, we employ a gold plasmonic nanopore to monitor the unfolding of SM bovine serum albumin (BSA). The gradual collapse of the BSA structure induced by high bias voltages is demonstrated through an increase in the fraction current blockade. Surface-enhanced Raman scattering (SERS) spectra provide structural evidence for protein unfolding, while the optical force is verified as an additional factor contributing to BSA deformation. The effect of the optical force on the dwell time of BSA in a nanopore is also investigated. The present study reveals that plasmonic nanopores offer multidimensional observations on the structure and conformation of SM proteins, which will drive further innovations in protein detection and analysis.
在单分子水平上直接检测蛋白质，尤其是其构象和构型信息，在各个生物技术领域都具有挑战性。等离子体纳米孔作为具有单分子（SM）灵敏度的多维生物传感器受到了关注。在这里，我们使用金等离子体纳米孔来监测单分子牛血清白蛋白（BSA）的展开。通过分数电流阻塞的增加证明了高偏置电压引起的BSA结构的逐渐坍塌。表面增强拉曼散射（SERS）光谱为蛋白质展开提供了结构证据，而光力被确认为导致BSA变形的另一个因素。还研究了光力对BSA在纳米孔中停留时间的影响。本研究表明，等离子体纳米孔提供了对单分子蛋白质结构和构象的多维观察，这将推动蛋白质检测和分析的进一步创新。
