title: Surface Curvature Relation to Protein Adsorption for Carbon-based Nanomaterials.
abstract: The adsorption of proteins onto carbon-based nanomaterials (CBNs) is dictated by hydrophobic and π-π interactions between aliphatic and aromatic residues and the conjugated CBN surface. Accordingly, protein adsorption is highly sensitive to topological constraints imposed by CBN surface structure; in particular, adsorption capacity is thought to increase as the incident surface curvature decreases. In this work, we couple Molecular Dynamics (MD) simulations with fluorescence spectroscopy experiments to characterize this curvature dependence in detail for the model protein bovine serum albumin (BSA). By studying BSA adsorption onto carbon nanotubes of increasing radius (featuring descending local curvatures) and a flat graphene sheet, we confirm that adsorption capacity is indeed enhanced on flatter surfaces. Naïve fluorescence experiments featuring multi-walled carbon nanotubes (MWCNTs), however, conform to an opposing trend. To reconcile these observations, we conduct additional MD simulations with MWCNTs that match those prepared in experiments; such simulations indicate that increased mass to surface area ratios in multi-walled systems explain the observed discrepancies. In reduction, our work substantiates the inverse relationship between protein adsorption capacity and surface curvature and further demonstrates the need for subtle consideration in experimental and simulation design.
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: Yu
authors.initials: Y
authors.lastname: Chong
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: Cuicui
authors.initials: C
authors.lastname: Ge
authors.affiliation: IBM Thomas J. Watson Research Center, Yorktown Heights, NY 10598, USA.
authors.forename: Jeffrey K
authors.initials: JK
authors.lastname: Weber
authors.affiliation: IBM Thomas J. Watson Research Center, Yorktown Heights, NY 10598, USA.
authors.forename: David R
authors.initials: DR
authors.lastname: Bell
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; D002244:Carbon / Q000737:chemistry*; D008958:Models, Molecular; D049329:Nanostructures / Q000737:chemistry*; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D015203:Reproducibility of Results; D012710:Serum Albumin, Bovine / Q000737:chemistry; D013050:Spectrometry, Fluorescence; D013499:Surface Properties
chemical_list: D011506:Proteins; D012710:Serum Albumin, Bovine; D002244:Carbon