title: Revealing the role of oxidation state in interaction between nitro/amino-derived particulate matter and blood proteins.
abstract: Surface oxidation states of ultrafine particulate matter can influence the proinflammatory responses and reactive oxygen species levels in tissue. Surface active species of vehicle-emission soot can serve as electron transfer-mediators in mitochondrion. Revealing the role of surface oxidation state in particles-proteins interaction will promote the understanding on metabolism and toxicity. Here, the surface oxidation state was modeled by nitro/amino ligands on nanoparticles, the interaction with blood proteins were evaluated by capillary electrophoresis quantitatively. The nitro shown larger affinity than amino. On the other hand, the affinity to hemoglobin is 10(3) times larger than that to BSA. Further, molecular docking indicated the difference of binding intensity were mainly determined by hydrophobic forces and hydrogen bonds. These will deepen the quantitative understanding of protein-nanoparticles interaction from the perspective of surface chemical state.
authors.affiliation: Key Laboratory of Colloid and Interface Chemistry, Ministry of Education, Department of Chemistry, Shandong University, Jinan 250100, China.
authors.forename: Zhen
authors.initials: Z
authors.lastname: Liu
authors.affiliation: National Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, Beijing 100190, China.|University of Chinese Academy of Sciences, Beijing 100049, China.
authors.forename: Ping
authors.initials: P
authors.lastname: Li
authors.affiliation: Department of Pharmacy, Weifang Medical University, Weifang 261053, China.
authors.forename: Weiwei
authors.initials: W
authors.lastname: Bian
authors.affiliation: National Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, Beijing 100190, China.
authors.forename: Jingkai
authors.initials: J
authors.lastname: Yu
authors.affiliation: Key Laboratory of Colloid and Interface Chemistry, Ministry of Education, Department of Chemistry, Shandong University, Jinan 250100, China.
authors.forename: Jinhua
authors.initials: J
authors.lastname: Zhan
mesh_terms: D000814:Aniline Compounds / Q000737:chemistry / Q000494:pharmacology*; D001798:Blood Proteins / Q000737:chemistry* / Q000378:metabolism*; D019075:Electrophoresis, Capillary; D006046:Gold; D006860:Hydrogen Bonding; D057927:Hydrophobic and Hydrophilic Interactions; D053768:Metal Nanoparticles / Q000737:chemistry; D008958:Models, Molecular; D062105:Molecular Docking Simulation; D010084:Oxidation-Reduction; D010316:Particle Size; D011487:Protein Conformation; D017382:Reactive Oxygen Species / Q000378:metabolism; D053260:Soot / Q000032:analysis* / Q000494:pharmacology; D013438:Sulfhydryl Compounds / Q000737:chemistry / Q000494:pharmacology*; D001335:Vehicle Emissions / Q000032:analysis
chemical_list: D000814:Aniline Compounds; D001798:Blood Proteins; D017382:Reactive Oxygen Species; D053260:Soot; D013438:Sulfhydryl Compounds; D001335:Vehicle Emissions; C014712:4-nitrothiophenolate; D006046:Gold; C064316:4-aminothiophenol