Effects of Surface Compositional and Structural Heterogeneity on Nanoparticle–Protein Interactions: Different Protein Configurations

As nanoparticles (NPs) enter into biological systems, they are immediately exposed to a variety and concentration of proteins. The physicochemical interactions between proteins and NPs are influenced by the surface properties of the NPs. To identify the effects of NP surface heterogeneity, the inter...

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Bibliographic Details
Published in:ACS nano 2014-06, Vol.8 (6), p.5402-5412
Main Authors: Huang, Rixiang, Carney, Randy P, Ikuma, Kaoru, Stellacci, Francesco, Lau, Boris L. T
Format: Article
Language:English
Subjects:
Adsorption
Animals
Calorimetry
Cattle
Circular Dichroism
Gold
Gold - chemistry
Heterogeneity
Humans
Kinetics
Light
Metal Nanoparticles - chemistry
Nanoparticles - chemistry
Nanostructure
Nanotechnology - methods
Particle Size
Protein Interaction Mapping
Protein Structure, Secondary
Proteins
Scattering, Radiation
Serum albumin
Serum Albumin, Bovine - chemistry
Spectrometry, Fluorescence
Static Electricity
Surface chemistry
Surface Properties
Surface structure
Thermodynamics
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Summary:As nanoparticles (NPs) enter into biological systems, they are immediately exposed to a variety and concentration of proteins. The physicochemical interactions between proteins and NPs are influenced by the surface properties of the NPs. To identify the effects of NP surface heterogeneity, the interactions between bovine serum albumin (BSA) and gold NPs (AuNPs) with similar chemical composition but different surface structures were investigated. Different interaction modes and BSA conformations were studied by dynamic light scattering, circular dichroism spectroscopy, fluorescence quenching and isothermal titration calorimetry (ITC). Depending on the surface structure of AuNPs, BSA seems to adopt either a “side-on” or an “end-on” conformation on AuNPs. ITC demonstrated that the adsorption of BSA onto AuNPs with randomly distributed polar and nonpolar groups was primarily driven by electrostatic interaction, and all BSA were adsorbed in the same process. The adsorption of BSA onto AuNPs covered with alternating domains of polar and nonpolar groups was a combination of different interactions. Overall, the results of this study point to the potential for utilizing nanoscale manipulation of NP surfaces to control the resulting NP–protein interactions.
ISSN:1936-0851
1936-086X
DOI:10.1021/nn501203k