title: Measuring protein structure and stability of protein-nanoparticle systems with synchrotron radiation circular dichroism.
abstract: We measure the structural and stability changes of proteins at nanomolar concentration upon interaction with nanoparticles. Using synchrotron radiation circular dichroism (SRCD), we measure a decrease of 6 °C in the thermal unfolding of human serum albumin upon interaction with silver nanoparticles while this does not happen with gold. The use of SRCD allows measuring critical parameters on protein-nanoparticle interactions, and it will provide experimental data on the relative stability of key biological proteins for nanotoxicology.
authors.affiliation: European Commission, Joint Research Centre, Institute for Health and Consumer Protection I-21027, Ispra (VA), Italy.
authors.forename: Stefania
authors.initials: S
authors.lastname: Laera
authors.forename: Giacomo
authors.initials: G
authors.lastname: Ceccone
authors.forename: Francois
authors.initials: F
authors.lastname: Rossi
authors.forename: Douglas
authors.initials: D
authors.lastname: Gilliland
authors.forename: Rohanah
authors.initials: R
authors.lastname: Hussain
authors.forename: Giuliano
authors.initials: G
authors.lastname: Siligardi
authors.forename: Luigi
authors.initials: L
authors.lastname: Calzolai
mesh_terms: D002942:Circular Dichroism; D053768:Metal Nanoparticles; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*; D055672:Static Electricity; D017356:Synchrotrons
chemical_list: D011506:Proteins