Xu Joanna Xiuzhu, Fitzkee Nicholas C
Department of Chemistry, Mississippi State University, Starkville, MS, United States.
Front Physiol. 2021 Aug 17;12:715419. doi: 10.3389/fphys.2021.715419. eCollection 2021.
The spontaneous formation of a protein corona on a nanoparticle surface influences the physiological success or failure of the synthetic nanoparticle as a drug carrier or imaging agent used . A quantitative understanding of protein-nanoparticle interactions is therefore critical for the development of nanoparticle-based therapeutics. In this perspective, we briefly discuss the challenges and limitations of current approaches used for studying protein-nanoparticle binding in a realistic biological medium. Subsequently, we demonstrate that solution nuclear magnetic resonance (NMR) spectroscopy is a powerful tool to monitor protein competitive binding in a complex serum medium . Importantly, when many serum proteins are competing for a gold nanoparticle (AuNP) surface, solution NMR is able to detect differences in binding thermodynamics, and kinetics of a tagged protein. Combined with other experimental approaches, solution NMR is an invaluable tool to understand protein behavior in the nanoparticle corona.
纳米颗粒表面蛋白质冠层的自发形成会影响合成纳米颗粒作为药物载体或成像剂在生理上的成败。因此，对蛋白质与纳米颗粒相互作用的定量理解对于基于纳米颗粒的治疗方法的开发至关重要。从这个角度来看，我们简要讨论了当前用于在实际生物介质中研究蛋白质与纳米颗粒结合的方法所面临的挑战和局限性。随后，我们证明溶液核磁共振（NMR）光谱是监测复杂血清介质中蛋白质竞争性结合的有力工具。重要的是，当许多血清蛋白竞争金纳米颗粒（AuNP）表面时，溶液NMR能够检测到标记蛋白结合热力学和动力学的差异。结合其他实验方法，溶液NMR是理解纳米颗粒冠层中蛋白质行为的宝贵工具。
