Dynamic light scattering for gold nanorod size characterization and study of nanorod-protein interactions

    Authors

    H. L. Liu; N. Pierre-Pierre;Q. Huo

    Comments

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    Abbreviated Journal Title

    Gold Bull.

    Keywords

    Gold nanoparticle; Gold nanorod; Protein interaction; Dynamic light; scattering; OPTICAL-PROPERTIES; BIOMEDICAL APPLICATIONS; CONTRAST AGENTS; NANOPARTICLES; NANOSTRUCTURES; IMMUNOASSAY; ABSORPTION; ALBUMIN; ASSAY; SHAPE; Chemistry, Inorganic & Nuclear; Chemistry, Physical; Materials Science, ; Multidisciplinary

    Abstract

    In recent years, there has been considerable interest and research activity in using gold nanoparticle materials for biomedical applications including biomolecular detection, bioimaging, drug delivery, and photothermal therapy. In order to apply gold nanoparticles in the real biological world, we need to have a better understanding of the potential interactions between gold nanoparticle materials and biomolecules in vivo and in vitro. Here, we report the use of dynamic light scattering (DLS) for gold nanorods characterization and nanorod-protein interaction study. In the size distribution diagram, gold nanorods with certain aspect ratios exhibit two size distribution peaks, one with an average hydrodynamic diameter at 5-7 nm, and one at 7080 nm. The small size peak is attributed to the rotational diffusion of the nanorods instead of an actual dimension of the nanorods. When proteins are adsorbed to the gold nanorods, the average particle size of the nanorods increases and the rotational diffusion-related size distribution peak also changes dramatically. We examined the interaction between four different proteins, bovine serum albumin, human serum albumin, immunoglobulin G, and immunoglobulin A (IgA) with four gold nanorods that have the same diameter but different aspect ratios. From this study, we found that protein adsorption to gold nanorods is strongly dependent on the aspect ratio of the nanorods, and varies significantly from protein to protein. The two serum albumin proteins caused nanorod aggregation upon interaction with the nanorods, while the two immunoglobulin proteins formed a stable protein corona on the nanorod surface without causing significant nanorod aggregation. This study demonstrates that DLS is a valuable tool for nanorod characterization. It reveals information complementary to molecular spectroscopic techniques on gold nanorod-protein interactions.

    Journal Title

    Gold Bulletin

    Volume

    45

    Issue/Number

    4

    Publication Date

    1-1-2012

    Document Type

    Article

    Language

    English

    First Page

    187

    Last Page

    195

    WOS Identifier

    WOS:000311962000002

    ISSN

    0017-1557

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