title: The role of basic residues in the adsorption of blood proteins onto the graphene surface.
abstract: With its many unique properties, graphene has shown great potential in various biomedical applications, while its biocompatibility has also attracted growing concerns. Previous studies have shown that the formation of protein-graphene corona could effectively reduce its cytotoxicity; however, the underlying molecular mechanism remains not well-understood. Herein, we use extensive molecular dynamics simulations to demonstrate that blood proteins such as bovine fibrinogen (BFG) can absorb onto the graphene surface quickly and tightly to form a corona complex. Aromatic residues contributed significantly during this adsorption process due to the strong π-π stacking interactions between their aromatic rings and the graphene sp(2)-carbons. Somewhat surprisingly, basic residues like arginine, also played an equally or even stronger role during this process. The strong dispersion interactions between the sidechains of these solvent-exposed basic residues and the graphene surface provide the driving force for a tight binding of these basic residues. To the best of our knowledge, this is the first study with blood proteins to show that, in addition to the aromatic residues, the basic residues also play an important role in the formation of protein-graphene corona complexes.
authors.affiliation: Institute of Quantitative Biology and Medicine, SRMP and RAD-X, Collaborative Innovation Center of Radiation Medicine of Jiangsu Higher Education Institutions, Soochow University, Suzhou 215123, China.
authors.forename: Zonglin
authors.initials: Z
authors.lastname: Gu
authors.affiliation: Institute of Quantitative Biology and Medicine, SRMP and RAD-X, Collaborative Innovation Center of Radiation Medicine of Jiangsu Higher Education Institutions, Soochow University, Suzhou 215123, China.
authors.forename: Zaixing
authors.initials: Z
authors.lastname: Yang
authors.affiliation: Institute of Quantitative Biology and Medicine, SRMP and RAD-X, Collaborative Innovation Center of Radiation Medicine of Jiangsu Higher Education Institutions, Soochow University, Suzhou 215123, China.
authors.forename: Lingle
authors.initials: L
authors.lastname: Wang
authors.affiliation: Institute of Quantitative Biology and Medicine, SRMP and RAD-X, Collaborative Innovation Center of Radiation Medicine of Jiangsu Higher Education Institutions, Soochow University, Suzhou 215123, China.
authors.forename: Hong
authors.initials: H
authors.lastname: Zhou
authors.affiliation: IBM Thomas J. Watson Research Center, Yorktown Heights, NY 10598, USA.
authors.forename: Camilo A
authors.initials: CA
authors.lastname: Jimenez-Cruz
authors.affiliation: 1] Institute of Quantitative Biology and Medicine, SRMP and RAD-X, Collaborative Innovation Center of Radiation Medicine of Jiangsu Higher Education Institutions, Soochow University, Suzhou 215123, China [2] IBM Thomas J. Watson Research Center, Yorktown Heights, NY 10598, USA [3] Department of Chemistry, Columbia University, New York, NY 10027, USA.
authors.forename: Ruhong
authors.initials: R
authors.lastname: Zhou
mesh_terms: D000327:Adsorption; D000818:Animals; D001798:Blood Proteins / Q000737:chemistry*; D002417:Cattle; D006108:Graphite / Q000737:chemistry*; D008958:Models, Molecular; D049329:Nanostructures / Q000737:chemistry; D011487:Protein Conformation; D013499:Surface Properties; D013997:Time Factors
chemical_list: D001798:Blood Proteins; D006108:Graphite