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.
Adsorbed protein
Biological identity
CD-UV spectroscopy
IR spectroscopy
Nanohydroxyapatite
Protein conformation
Surface structure
Zeta-Potential
Journal
Colloids and surfaces. B, Biointerfaces
ISSN: 1873-4367
Titre abrégé: Colloids Surf B Biointerfaces
Pays: Netherlands
ID NLM: 9315133
Informations de publication
Date de publication:
Apr 2020
Apr 2020
Historique:
received:
25
07
2019
revised:
18
12
2019
accepted:
04
01
2020
pubmed:
1
2
2020
medline:
26
9
2020
entrez:
1
2
2020
Statut:
ppublish
Résumé
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).
Identifiants
pubmed: 32004906
pii: S0927-7765(20)30010-2
doi: 10.1016/j.colsurfb.2020.110780
pii:
doi:
Substances chimiques
Serum Albumin, Bovine
27432CM55Q
Durapatite
91D9GV0Z28
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
110780Informations de copyright
Copyright © 2020 Elsevier B.V. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.