蛋白质冠的热力学与分子图景

摘要(中文译文)

蛋白质冠重新定义了纳米颗粒的界面身份，并决定其后续的生物学响应。然而，支配其形成及单颗粒水平时空演化的热力学原理仍未被充分阐明。为解决这一问题，我们开发了一个集成的表面等离激元成像与光镊平台，用于实时、无标记地追踪单个金纳米颗粒（AuNPs）上蛋白质冠的组装过程。通过精确调控局部温度和pH，我们证明蛋白质冠的形成可由界面自由能最小化驱动，并与蛋白质分子重排相耦合。动力学分析揭示了不同的吸附机制：牛血清白蛋白（BSA）遵循Lagergren准一级动力学，而四聚体血红蛋白（Hb）则表现为准二级行为，反映了分子堆积和结构稳定性的差异。此外，对IgG/抗IgG相互作用的单分子涨落解析表明，蛋白质冠显著抑制了热涨落并限制了构象转变。

Abstract

The protein corona redefines interfacial identity and dictates subsequent biological responses of nanoparticles. Nevertheless, the thermodynamic principles governing its formation and spatiotemporal evolution at the single-particle level remain poorly resolved. To address this, we developed an integrated surface plasmonic imaging and optical tweezing platform for real-time, label-free tracking of protein corona assembly on individual Au nanoparticles (AuNPs). By precise modulation of local temperature and pH, we demonstrated that corona formation can be energetically driven by minimization of interfacial free energy and coupled with protein molecule rearrangements. Kinetic analyses revealed distinct adsorption mechanisms: bovine serum albumin (BSA) followed Lagergren pseudo-first-order kinetics, whereas tetrameric hemoglobin (Hb) exhibited pseudo-second-order behavior, reflecting differences in molecular packing and structural stability. Furthermore, single-molecule fluctuation dissection of IgG/anti-IgG interactions revealed that the protein corona significantly quenched thermal fluctuations and restricted configurational transitions.

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