The effect of surface nanometre-scale morphology on protein adsorption.
BACKGROUND
Protein adsorption is the first of a complex series of events that regulates many phenomena at the nano-bio interface, e.g. cell adhesion and differentiation, in vivo inflammatory responses and protein crystallization. A quantitative understanding of how nanoscale morphology influences protein adsorption is strategic for providing insight into all of these processes, however this understanding has been lacking until now.


RESULTS
Here we introduce novel methods for quantitative high-throughput characterization of protein-surface interaction and we apply them in an integrated experimental strategy, to study the adsorption of a panel of proteins on nanostructured surfaces. We show that the increase of nanoscale roughness (from 15 nm to 30 nm) induces a decrease of protein binding affinity (<or=90%) and a relevant increase in adsorbed proteins (<or=500%) beyond the corresponding increase of specific area. We demonstrate that these effects are caused by protein nucleation on the surface, which is promoted by surface nanoscale pores.


CONCLUSIONS
These results show that the adsorption of proteins depends significantly on surface nanostructure and that the relevant morphological parameter regulating the protein adsorption process is the nanometric pore shape. These new findings improve our understanding of the role of nanostructures as a biomaterial design parameter and they have important implications for the general understanding of cell behavior on nanostructured surfaces.
Scopelliti
Pasquale Emanuele
PE
Interdisciplinary Centre for Nanostructured Materials and Interfaces (CIMaINa) and Physics Department, Università degli studi di Milano, Milan, Italy.
Borgonovo
Antonio
A
Indrieri
Marco
M
Giorgetti
Luca
L
Bongiorno
Gero
G
Carbone
Roberta
R
Podestà
Alessandro
A
Milani
Paolo
P
D000327:Adsorption; D049329:Nanostructures / Q000737:chemistry*; D036103:Nanotechnology / Q000379:methods; D011506:Proteins / Q000737:chemistry*; D013499:Surface Properties
D011506:Proteins