Presenting Precision Glycomacromolecules on Gold Nanoparticles for Increased Lectin Binding

• Published in: Polymers Vol. 9; no. 12; p. 716
• Main Authors: Boden, Sophia, Wagner, Kristina G, Karg, Matthias, Hartmann, Laura
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 14.12.2017; MDPI
• Subjects: Aliphatic compounds; Binding; Biosensors; Buffer solutions; Carbohydrates; Chemical synthesis; Con A; Concanavalin A; Ethylene glycol; glyco-gold nanoparticles; Gold; Hydrophobicity; Lectins; Ligands; Nanoparticles; Photon correlation spectroscopy; precision glycomacromolecules; Receptors; Resonance scattering; SPR; glyco-gold nanoparticles; SPR; precision glycomacromolecules; Con A
• ISSN: 2073-4360; 2073-4360
• DOI: 10.3390/polym9120716

Glyco-functionalized gold nanoparticles have great potential as biosensors and as inhibitors due to their increased binding to carbohydrate-recognizing receptors such as the lectins. Here we apply previously developed solid phase polymer synthesis to obtain a series of precision glycomacromolecules that allows for straightforward variation of their chemical structure as well as functionalization of gold nanoparticles by ligand exchange. A novel building block is introduced allowing for the change of spacer building blocks within the macromolecular scaffold going from an ethylene glycol unit to an aliphatic spacer. Furthermore, the valency and overall length of the glycomacromolecule is varied. All glyco-functionalized gold nanoparticles show high degree of functionalization along with high stability in buffer solution. Therefore, a series of measurements applying UV-Vis spectroscopy, dynamic light scattering (DLS) and surface plasmon resonance (SPR) were performed studying the aggregation behavior of the glyco-functionalized gold nanoparticles in presence of model lectin Concanavalin A. While the multivalent presentation of glycomacromolecules on gold nanoparticles (AuNPs) showed a strong increase in binding compared to the free ligands, we also observed an influence of the chemical structure of the ligand such as its valency or hydrophobicity on the resulting lectin interactions. The straightforward variation of the chemical structure of the precision glycomacromolecule thus gives access to tailor-made glyco-gold nanoparticles (glyco-AuNPs) and fine-tuning of their lectin binding properties.