Binding of Human Serum Albumin to Single-Walled Carbon Nanotubes Activated Neutrophils to Increase Production of Hypochlorous Acid, the Oxidant Capable of Degrading Nanotubes

作者：Lu, Naihao^*; Li, Jiayu; Tian, Rong; Peng, Yi-Yuan

来源：Chemical Research in Toxicology, 2014, 27(6): 1070-1077.

DOI：10.1021/tx5001317

• OXIDATIVE STRESS
• MAMMALIAN-CELLS
• MYELOPEROXIDASE
• BIODEGRADATION
• PROTEINS
• NANOMATERIALS
• MECHANISMS
• TOXICITY
• INFLAMMATION
• MACROPHAGES

Previous studies have shown that carboxylated single-walled carbon nanotubes (SWCNTs) can be catalytically biodegraded by hypochlorite (OCl-) and reactive radical intermediates of the human neutrophil enzyme myeloperoxidase (MPO). However, the importance of protein-SWCNT interactions in the biodegradation of SWCNTs was not stressed. Here, we used both experimental and theoretical approaches to investigate the interactions of SWCNTs with human serum albumin (HSA, one of the most abundant proteins in blood circulation) and found that the binding was involved in the electrostatic interactions of positively charged Arg residues of HSA with the carboxyls on the nanotubes, along with the pi-pi stacking interactions between SWCNTs and aromatic Tyr residues in HSA. Compared with SWCNTs, the binding of HSA could result in a reduced effect for OCl- (or the human MPO system)-induced SWCNTs degradation in vitro. However, the HSA-SWCNT interactions would enhance cellular uptake of nanotubes and stimulate MPO release and OCl- generation in neutrophils, thereby creating the conditions favorable for the degradation of the nanotubes. Upon zymosan stimulation, both SWCNTs and HSA-SWCNTs were significantly biodegraded in neutrophils, and the degree of biodegradation was more for HSA-SWCNTs under these relevant in vivo conditions. Our findings suggest that the binding of HSA may be an important determinant for MPO-mediated SWCNT biodegradation in human inflammatory cells and therefore shed light on the biomedical and biotechnological applications of safe carbon nanotubes by comprehensive preconsideration of their interactions with human serum proteins.

• 出版日期2014-6
• 单位江西师范大学