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Self-assembly and characterization of transferrin-gold nanoconstructs and their interaction with bio-interfaces

Year: 2015

Journal: NANOSCALE, Vol. 7, p 8062-8070, 20170208

Authors: McDonagh, Birgitte H.; Volden, Sondre; Lystvet, Sina M.; Singh, Gurvinder; Ese, Marit-Helen G.; Ryan, Joseph A.; Lindgren, Mikael; Sandvig, Axel; Sandvig, Ioanna; Glomm, Wilhelm R.

Organizations: Norwegian Univ Sci & Technol NTNU, Dept Chem Engn, Ugelstad Lab, N-7491 Trondheim, Norway; Norwegian Univ Sci & Technol NTNU, Dept Mat Sci & Engn, N-7491 Trondheim, Norway; SINTEF Energy Res, N-7465 Trondheim, Norway; Iona Coll, Dept Chem, New Rochelle, NY USA; Norwegian Univ Sci & Technol NTNU, Dept Phys, N-7491 Trondheim, Norway; Umea Univ, Dept Neurosurg, Div Pharmacol & Clin Neurosci, S-90187 Umea, Sweden; Norwegian Univ Sci & Technol NTNU, Fac Med, Dept Neurosci, N-7491 Trondheim, Norway; Univ Cambridge, Dept Clin Neurosci, John Van Geest Ctr Brain Repair, Cambridge CB2 0PY, England; SINTEF Mat & Chem, Sect Biotechnol & Nanomed, Trondheim, Norway

Transferrin (Tf) conjugated to gold nanoparticles and clusters combine the protein's site-specific receptor targeting capabilities with the optical properties imparted by the nano-sized gold. We have described two different synthesis protocols, one yielding fluorescent Tf-stabilized gold nanoclusters (AuNCs) and one yielding Tf-stabilized gold nanoparticles that exhibit localized surface plasmon resonance. We demonstrate that the synthetic route employed has a large influence both on the gold nanostructure formed, and also on the structural integrity of the protein. A slight protein unfolding allows stronger interaction with lipids, and was found to significantly perturb lipid monolayers. Interactions between the protein-gold nanostructures and three different cell types were also assessed, indicating that the enhanced membrane affinity may be attributed to intercellular membrane differences.