Ontology highlight
ABSTRACT: 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.Methodology/principal findings
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 (
SUBMITTER: Scopelliti PE
PROVIDER: S-EPMC2912332 | biostudies-literature | 2010 Jul
REPOSITORIES: biostudies-literature
Scopelliti Pasquale Emanuele PE Borgonovo Antonio A Indrieri Marco M Giorgetti Luca L Bongiorno Gero G Carbone Roberta R Podestà Alessandro A Milani Paolo P
PloS one 20100729 7
<h4>Background</h4>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.<h4>Methodology/principal findings</h4>Here we introduce ...[more]