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Updated: Jun 10, 2026
Monitoring Protein Adsorption with Solid-state Nanopores
Published on: December 2, 2011
The effect of surface nanometre-scale morphology on protein adsorption
Pasquale Emanuele Scopelliti1, Antonio Borgonovo, Marco Indrieri
1Interdisciplinary Centre for Nanostructured Materials and Interfaces (CIMaINa) and Physics Department, Università degli studi di Milano, Milan, Italy.
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 (
Conclusions/Significance:
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.
