Source abstract
Abstract
Meeting proteins is regarded as the starting event for nanostructures to enter biological systems. Understanding their interactions is thus essential for a newly emerging field, nanomedicine. Chemically converted graphene (CCG) is a wonderful two‐dimesional (2D) material for nanomedecine, but its stability in biological environments is limited. Systematic probing on the binding of proteins to CCG is currently lacking. Herein, we report a comprehensive study on the interactions between blood proteins and stabilized CCG (sCCG). CCG nanosheets are functionalized by monolayers of perylene leading to significant improvement in their resistance to electrolyte salts and long‐term stability, but retain their core structural characteristics. Five types of model human blood proteins including human fibrinogen, γ‐globulin, bovine serum albumin (BSA), insulin, and histone are tested. The main drving forces for blood protein binding involve the π–π interacations between the π‐plane of sCCG and surface aromatic amonic acid (sAA) residues of proteins. Several key binding parameters including the binding amount, Hill coefficient, and binding constant are determined. Through a detailed analysis of key controlling factors, we conclude that the protein binding to sCCG is determined mainly by the protein size, the number, and the density of the sAA.
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Affiliations
Department of Chemistry Technical University of Denmark DK‐2800 Kongens Lyngby Denmark
Engineering Laboratory for Modern Analytical Techniques c/o State Key Laboratory of Electroanalytical Chemistry Changchun Institute of Applied Chemistry Chinese Academy of Sciences Changchun 130022 P. R. China
University of Chinese Academy of Sciences Beijing 100049 P. R. China
Funding
Danish Research Council for Technology and Product Science · European Framework Program-Marie Curie Actions under the ELECTRONANOMAT · National Science Foundation of China · Department of Science and Technology of Jilin Province