Towards the control of the biological identity of nanobiomaterials: Impact of the structure of 011¯0 surface terminations of nanohydroxyapatite on the conformation of adsorbed proteins

• Published in: Colloids and surfaces, B, Biointerfaces Vol. 188; p. 110780
• Main Authors: Catalano, Federico, Ivanchenko, Pavlo, Rebba, Erica, Sakhno, Yuriy, Alberto, Gabriele, Dovbeshko, Galyna, Martra, Gianmario
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.04.2020
• Subjects: Adsorbed protein; Biological identity; CD-UV spectroscopy; IR spectroscopy; Nanohydroxyapatite; Protein conformation; Surface structure; Zeta-Potential; Biological identity; CD-UV spectroscopy; Adsorbed protein; Protein conformation; Zeta-Potential; Nanohydroxyapatite; IR spectroscopy; Surface structure
• ISSN: 0927-7765; 1873-4367
• DOI: 10.1016/j.colsurfb.2020.110780

[Display omitted] •The protein coverage cannot be calculated using the SSA of dry nanoparticles.•BSA has strong affinity towards 011¯0 surfaces of nano-hydroxyapatite particles.•Interactions among adsorbed proteins can be detected by CD-UV spectroscopy.•The structure of adsorbed proteins depends on the surface structure of nano-HA. High-resolution transmission electron microscopy, ζ-potential and in-situ IR spectroscopy of adsorbed CO were combined for elucidating the ratio between  {011¯0}_ Ca-rich: {011¯0}_ P-rich terminations of  {011¯0} facets, i.e. the surfaces with the highest morphological importance, in two nanohydroxyapatite samples. Bovine serum albumin was found to form at least a monolayer on the surface left accessible to protein molecules by the agglomeration of nanoparticles when suspended in the buffered incubation medium. Noticeably, the conformation of adsorbed proteins appeared sensitive to the ratio between the two types of  {011¯0} terminations, also resulting in a difference in the surface exposed toward the exterior by the adsorbed protein layer(s).