title: Binding of blood proteins to carbon nanotubes reduces cytotoxicity.
abstract: With the potential wide uses of nanoparticles such as carbon nanotubes in biomedical applications, and the growing concerns of nanotoxicity of these engineered nanoparticles, the importance of nanoparticle-protein interactions cannot be stressed enough. In this study, we use both experimental and theoretical approaches, including atomic force microscope images, fluorescence spectroscopy, CD, SDS-PAGE, and molecular dynamics simulations, to investigate the interactions of single-wall carbon nanotubes (SWCNTs) with human serum proteins, and find a competitive binding of these proteins with different adsorption capacity and packing modes. The π-π stacking interactions between SWCNTs and aromatic residues (Trp, Phe, Tyr) are found to play a critical role in determining their adsorption capacity. Additional cellular cytotoxicity assays, with human acute monocytic leukemia cell line and human umbilical vein endothelial cells, reveal that the competitive bindings of blood proteins on the SWCNT surface can greatly alter their cellular interaction pathways and result in much reduced cytotoxicity for these protein-coated SWCNTs, according to their respective adsorption capacity. These findings have shed light toward the design of safe carbon nanotube nanomaterials by comprehensive preconsideration of their interactions with human serum proteins.
authors.affiliation: Chinese Academy of Sciences Key Lab for Biomedical Effects of Nanomaterials and Nanosafety, National Center for Nanoscience and Technology, Institute of High Energy Physics, Chinese Academy of Sciences, Beijing 100190, China.
authors.forename: Cuicui
authors.initials: C
authors.lastname: Ge
authors.forename: Jiangfeng
authors.initials: J
authors.lastname: Du
authors.forename: Lina
authors.initials: L
authors.lastname: Zhao
authors.forename: Liming
authors.initials: L
authors.lastname: Wang
authors.forename: Ying
authors.initials: Y
authors.lastname: Liu
authors.forename: Denghua
authors.initials: D
authors.lastname: Li
authors.forename: Yanlian
authors.initials: Y
authors.lastname: Yang
authors.forename: Ruhong
authors.initials: R
authors.lastname: Zhou
authors.forename: Yuliang
authors.initials: Y
authors.lastname: Zhao
authors.forename: Zhifang
authors.initials: Z
authors.lastname: Chai
authors.forename: Chunying
authors.initials: C
authors.lastname: Chen
mesh_terms: D000327:Adsorption; D024322:Amino Acids, Aromatic / Q000737:chemistry; D000818:Animals; D001665:Binding Sites; D001798:Blood Proteins / Q000737:chemistry / Q000187:drug effects / Q000378:metabolism*; D002417:Cattle; D002460:Cell Line; D049109:Cell Proliferation / Q000187:drug effects; D002470:Cell Survival / Q000187:drug effects; D005340:Fibrinogen / Q000737:chemistry / Q000378:metabolism; D061307:Human Umbilical Vein Endothelial Cells; D006801:Humans; D066298:In Vitro Techniques; D018625:Microscopy, Atomic Force; D008958:Models, Molecular; D056004:Molecular Dynamics Simulation; D037742:Nanotubes, Carbon / Q000737:chemistry* / Q000633:toxicity* / Q000648:ultrastructure; D011485:Protein Binding; D017433:Protein Structure, Secondary / Q000187:drug effects; D012710:Serum Albumin, Bovine / Q000737:chemistry / Q000378:metabolism; D005719:gamma-Globulins / Q000737:chemistry / Q000378:metabolism
chemical_list: D024322:Amino Acids, Aromatic; D001798:Blood Proteins; D037742:Nanotubes, Carbon; D005719:gamma-Globulins; D012710:Serum Albumin, Bovine; D005340:Fibrinogen