The effect of surface nanometre-scale morphology on protein adsorption.

<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 morp...

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Autores principales: Pasquale Emanuele Scopelliti, Antonio Borgonovo, Marco Indrieri, Luca Giorgetti, Gero Bongiorno, Roberta Carbone, Alessandro Podestà, Paolo Milani
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Publicado: Public Library of Science (PLoS) 2010
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Acceso en línea:https://doaj.org/article/fc158b717bd2402dab016192ad52986e
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spelling oai:doaj.org-article:fc158b717bd2402dab016192ad52986e2021-11-18T06:36:35ZThe effect of surface nanometre-scale morphology on protein adsorption.1932-620310.1371/journal.pone.0011862https://doaj.org/article/fc158b717bd2402dab016192ad52986e2010-07-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/20686681/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203<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 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.<h4>Conclusions/significance</h4>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.Pasquale Emanuele ScopellitiAntonio BorgonovoMarco IndrieriLuca GiorgettiGero BongiornoRoberta CarboneAlessandro PodestàPaolo MilaniPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 5, Iss 7, p e11862 (2010)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Pasquale Emanuele Scopelliti
Antonio Borgonovo
Marco Indrieri
Luca Giorgetti
Gero Bongiorno
Roberta Carbone
Alessandro Podestà
Paolo Milani
The effect of surface nanometre-scale morphology on protein adsorption.
description <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 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.<h4>Conclusions/significance</h4>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.
format article
author Pasquale Emanuele Scopelliti
Antonio Borgonovo
Marco Indrieri
Luca Giorgetti
Gero Bongiorno
Roberta Carbone
Alessandro Podestà
Paolo Milani
author_facet Pasquale Emanuele Scopelliti
Antonio Borgonovo
Marco Indrieri
Luca Giorgetti
Gero Bongiorno
Roberta Carbone
Alessandro Podestà
Paolo Milani
author_sort Pasquale Emanuele Scopelliti
title The effect of surface nanometre-scale morphology on protein adsorption.
title_short The effect of surface nanometre-scale morphology on protein adsorption.
title_full The effect of surface nanometre-scale morphology on protein adsorption.
title_fullStr The effect of surface nanometre-scale morphology on protein adsorption.
title_full_unstemmed The effect of surface nanometre-scale morphology on protein adsorption.
title_sort effect of surface nanometre-scale morphology on protein adsorption.
publisher Public Library of Science (PLoS)
publishDate 2010
url https://doaj.org/article/fc158b717bd2402dab016192ad52986e
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