Protein-nanoparticle interactions

the effects of surface compositional and structural heterogeneity are scale dependent.

Rixiang Huang, Randy P. Carney, Francesco Stellacci, Boris L T Lau

Research output: Contribution to journalArticle

65 Citations (Scopus)

Abstract

Nanoparticles (NPs) in the biological environment are exposed to a large variety and concentration of proteins. Proteins are known to adsorb in a 'corona' like structure on the surface of NPs. In this study, we focus on the effects of surface compositional and structural heterogeneity on protein adsorption by examining the interaction of self-assembled monolayer coated gold NPs (AuNPs) with two types of proteins: ubiquitin and fibrinogen. This work was designed to systematically investigate the role of surface heterogeneity in nanoparticle-protein interaction. We have chosen the particles as well as the proteins to provide different types (in distribution and length-scale) of heterogeneity. The goal was to unveil the role of heterogeneity and of its length-scale in the particle-protein interaction. Dynamic light scattering and circular dichroism spectroscopy were used to reveal different interactions at pH above and below the isoelectric points of the proteins, which is related to the charge heterogeneity on the protein surface. At pH 7.4, there was only a monolayer of proteins adsorbed onto the NPs and the secondary structure of proteins remained intact. At pH 4.0, large aggregates of nanoparticle-protein complexes were formed and the secondary structures of the proteins were significantly disrupted. In terms of interaction thermodynamics, results from isothermal titration calorimetry showed that ubiquitin adsorbed differently onto (1) AuNPs with charged and nonpolar terminals organized into nano-scale structure (66-34 OT), (2) AuNPs with randomly distributed terminals (66-34 brOT), and (3) AuNPs with homogeneously charged terminals (MUS). This difference in adsorption behavior was not observed when AuNPs interacted with fibrinogen. The results suggested that the interaction between the proteins and AuNPs was influenced by the surface heterogeneity on the AuNPs, and this influence depends on the scale of surface heterogeneity and the size of the proteins.

Original languageEnglish
Pages (from-to)6928-6935
Number of pages8
JournalNanoscale
Volume5
Issue number15
Publication statusPublished - Aug 7 2013

Fingerprint

Nanoparticles
Proteins
Secondary Protein Structure
Ubiquitin
Fibrinogen
Adsorption
Calorimetry
Isoelectric Point
Circular dichroism spectroscopy
Circular Dichroism
Thermodynamics
Gold
Self assembled monolayers
Spectrum Analysis
Dynamic light scattering
Membrane Proteins
Titration
Monolayers

ASJC Scopus subject areas

  • Materials Science(all)
  • Medicine(all)

Cite this

Protein-nanoparticle interactions : the effects of surface compositional and structural heterogeneity are scale dependent. / Huang, Rixiang; Carney, Randy P.; Stellacci, Francesco; Lau, Boris L T.

In: Nanoscale, Vol. 5, No. 15, 07.08.2013, p. 6928-6935.

Research output: Contribution to journalArticle

Huang, R, Carney, RP, Stellacci, F & Lau, BLT 2013, 'Protein-nanoparticle interactions: the effects of surface compositional and structural heterogeneity are scale dependent.', Nanoscale, vol. 5, no. 15, pp. 6928-6935.
Huang, Rixiang ; Carney, Randy P. ; Stellacci, Francesco ; Lau, Boris L T. / Protein-nanoparticle interactions : the effects of surface compositional and structural heterogeneity are scale dependent. In: Nanoscale. 2013 ; Vol. 5, No. 15. pp. 6928-6935.
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