We report on a systematic investigation of molecular conjugation of tumor necrosis factor protein-a (TNF) onto gold nanoparticles (AuNPs) and the subsequent binding behavior to its antibody (anti-TNF), by employing a combination of physical and spectroscopic characterization methods. Dodecyl sulfate ions induce desorption of monomeric TNF from the AuNP surface, indicating a relatively weak intermolecular binding within the AuNP-bound TNF trimers. Anti-TNF binds to both TNF-conjugated and citrate-stabilized AuNPs, showing that non-specific binding is significant. The inclusion of thiolated polyethylene glycol (SH-PEG) on the AuNPs inhibits the binding of anti-TNF, and the amount of inhibition is related to the number ratio of surface bound SH-PEG to TNF and the way in which the ligands are introduced. This study highlights the challenges in quantitatively characterizing complex hybrid nanoscale conjugates, and provides insight on TNF-AuNP formation and activity.

Tumor necrosis factor interaction with gold nanoparticles

244th National Meeting (2012)

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