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

被引:10
|
作者
McDonagh, Birgitte H. [1 ]
Volden, Sondre [1 ]
Lystvet, Sina M. [1 ]
Singh, Gurvinder [2 ]
Ese, Marit-Helen G. [3 ]
Ryan, Joseph A. [4 ]
Lindgren, Mikael [5 ]
Sandvig, Axel [6 ,7 ]
Sandvig, Ioanna [7 ,8 ]
Glomm, Wilhelm R. [1 ,9 ]
机构
[1] Norwegian Univ Sci & Technol NTNU, Dept Chem Engn, Ugelstad Lab, N-7491 Trondheim, Norway
[2] Norwegian Univ Sci & Technol NTNU, Dept Mat Sci & Engn, N-7491 Trondheim, Norway
[3] SINTEF Energy Res, N-7465 Trondheim, Norway
[4] Iona Coll, Dept Chem, New Rochelle, NY USA
[5] Norwegian Univ Sci & Technol NTNU, Dept Phys, N-7491 Trondheim, Norway
[6] Umea Univ, Dept Neurosurg, Div Pharmacol & Clin Neurosci, S-90187 Umea, Sweden
[7] Norwegian Univ Sci & Technol NTNU, Fac Med, Dept Neurosci, N-7491 Trondheim, Norway
[8] Univ Cambridge, Dept Clin Neurosci, John Van Geest Ctr Brain Repair, Cambridge CB2 0PY, England
[9] SINTEF Mat & Chem, Sect Biotechnol & Nanomed, Trondheim, Norway
关键词
DRUG-DELIVERY; CLUSTERS;
D O I
10.1039/c5nr01284h
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
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.
引用
收藏
页码:8062 / 8070
页数:9
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