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    Gold Nanoparticles Affect Thermoresponse and Aggregation Properties of Mesoscopic Immunoglobulin G Clusters

    Year: 2011

    Journal: J. Phys. Chem. C, 2011, 115 (23), pp 11390–11399, 20110906

    Authors: Volden S. †, Trinh L.T.T. ‡, Kjøniksen A-L ‡§, Yasuda M., Nyström B. ‡, Glomm W.R. *†

    Last authors: Wilhelm R. Glomm

    Organizations: † Ugelstad Laboratory, Department of Chemical Engineering, Norwegian University of Science and Technology (NTNU), N-7491 Trondheim, Norway ‡ Department of Chemistry, University of Oslo, P.O.Box 1033, N-0315 Oslo, Norway § Department of Pharmacy, School of Pharmacy, University of Oslo, P.O. Box 1068, N-0316 Oslo, Norway Department of Chemical Engineering, Osaka Prefecture University, 1-1 Gakuen-cho, Sakai, 5998531 Osaka, Japan

    Country: Norway, Japan

    Conjugation of proteins to nanomaterials such as gold nanoparticles (Aunp) is known to modulate the flocculation state, conformation, and functionality of the adsorbed protein. However, these changes in the adsorbed protein are also expected to manifest themselves in the temperature response relative to the native protein. Here, we have studied the thermoresponse of Aunp–Immunoglobulin G (Aunp–IgG) constructs in the temperature range between 25 and 60 °C using UV–vis and fluorescence spectroscopies, quartz crystal microbalance with dissipation monitoring (QCM-D), and dynamic light scattering (DLS). Under the conditions studied here, IgG forms multilayers on planar gold surfaces, whereas Aunps are embedded in mesoscopic protein clusters. We demonstrate that Aunp–IgG systems display irreversible temperature-induced blue shifts and narrowing of the localized surface plasmon resonance (LSPR), which corresponds to a gradual breakup of Aunp–IgG clusters, as corroborated by DLS, steady-state (using both intrinsic and extrinsic probes), and time-resolved fluorescence. The modulation of thermal response depends on size of the Aunp core (30 or 80 nm), with the observed LSPR behavior being discussed within the framework of Mie–Drude theory. The findings presented here reveal that temperature response of Aunp–IgG constructs cannot be assumed to mirror that of the native protein.