We propose a novel method for determining the structural and thermodynamic properties of nanoparticle- protein complexes under physiological conditions. The method consists of collecting a full set of small-angle X-ray and neutron-scattering measurements in solutions with different concentrations of nanoparticles and protein. The nanoparticle-protein dissociation process is described in the framework of the Hill cooperative model, based on which the whole set of X-ray and neutron-scattering data is fitted simultaneously. This method is applied to water solutions of gold nanoparticles in the presence of human serum albumin without any previous manipulation and can be, in principle, extended to all systems. We demonstrate that the protein dissociation constant, the Hill coefficient, and the stoichiometry of the nanoparticle-protein complex are obtained with a high degree of confidence.

Structural and Thermodynamic Properties of Nanoparticle-Protein Complexes: A Combined SAXS and SANS Study / Spinozzi, Francesco; Ceccone, Giacomo; Moretti, Paolo; Campanella, Gabriele; Ferrero, Claudio; Combet, Sophie; Ojea Jimenez, Isaac; Ghigna, Paolo. - In: LANGMUIR. - ISSN 0743-7463. - STAMPA. - 33:9(2017), pp. 2248-2256. [10.1021/acs.langmuir.6b04072]

Structural and Thermodynamic Properties of Nanoparticle-Protein Complexes: A Combined SAXS and SANS Study

SPINOZZI, Francesco;MORETTI, PAOLO;
2017-01-01

Abstract

We propose a novel method for determining the structural and thermodynamic properties of nanoparticle- protein complexes under physiological conditions. The method consists of collecting a full set of small-angle X-ray and neutron-scattering measurements in solutions with different concentrations of nanoparticles and protein. The nanoparticle-protein dissociation process is described in the framework of the Hill cooperative model, based on which the whole set of X-ray and neutron-scattering data is fitted simultaneously. This method is applied to water solutions of gold nanoparticles in the presence of human serum albumin without any previous manipulation and can be, in principle, extended to all systems. We demonstrate that the protein dissociation constant, the Hill coefficient, and the stoichiometry of the nanoparticle-protein complex are obtained with a high degree of confidence.
2017
File in questo prodotto:
File Dimensione Formato  
spinozzi2017.pdf

solo utenti autorizzati

Descrizione: Articolo Principale
Tipologia: Documento in post-print (versione successiva alla peer review e accettata per la pubblicazione)
Licenza d'uso: Tutti i diritti riservati
Dimensione 1.35 MB
Formato Adobe PDF
1.35 MB Adobe PDF   Visualizza/Apri   Richiedi una copia
paper_Feb_3_3.pdf

accesso aperto

Tipologia: Documento in post-print (versione successiva alla peer review e accettata per la pubblicazione)
Licenza d'uso: Tutti i diritti riservati
Dimensione 3.21 MB
Formato Adobe PDF
3.21 MB Adobe PDF Visualizza/Apri

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11566/249100
Citazioni
  • ???jsp.display-item.citation.pmc??? 6
  • Scopus 23
  • ???jsp.display-item.citation.isi??? 21
social impact