Jiang Xiaoze, Housni Abdelghani, Gody Guillaume, Boullanger Paul, Charreyre Marie-Thérèse, Delair Thierry, Narain Ravin
Department of Chemical and Materials Engineering, University of Alberta, ECERF, Edmonton, Alberta T6G2G6, Canada, Department of Chemistry and Biochemistry, Laurentian University, 935, Ramsey Lake Road, P3E 2C6, ON, Canada, Unité Mixte CNRS-bioMérieux, Ecole Normale Supérieure de Lyon, IFR 128, 46 allée d'Italie, 69364 Lyon Cedex 07, France, and Laboratoire de Chimie Organique II, UMR 5622 CNRS/UCBL, 69616 Villeurbanne Cedex, France.
Bioconjug Chem. 2010 Mar 17;21(3):521-30. doi: 10.1021/bc900431p. Epub 2010 Feb 3.
Gold nanoparticles (NPs) functionalized with a mixed shell of well-defined biotinylated glycopolymers and polyethylene glycol (PEG) provide an effective platform for the biomolecular recognition of proteins both in solution and on surfaces. Well-defined biotinylated glycopolymers were first synthesized by the reversible addition-fragmentation chain transfer (RAFT) process. They contain two types of carbohydrate residues either N-acetyl β-D-glucosaminopyranoside (GlcNAc) or α-D-mannopyranoside (Man) as pendent groups. The biotinylated glycopolymers and polyethylene glycol were subsequently used in the in situ formation of gold glyconanoparticles via an easy photochemical process. The obtained biotinylated glyconanoparticles were characterized by dynamic light scattering (DLS) and transmission electron microscopy (TEM). The bioavailability of the biotin and specific carbohydrate residues at the periphery of the NPs were assessed using the diffraction optic technology (DOT) system. The studies showed the accessibility of the biotin ligands for conjugation to immobilized avidin on the DOTLab biosensor. Furthermore, these avidin conjugated glyconanoparticles were found to selectively immobilize lectins. The specificity of lectin binding was dependent on the type of carbohydrate residues. As such, N-acetyl β-D-glucosaminoside decorated gold nanoparticles were found to specifically interact with wheat germ agglutinin (WGA) lectin, whereas α-D-mannoside ones were found to specifically interact with Concanavalin A (Con A) lectin.
用具有明确结构的生物素化糖聚合物和聚乙二醇（PEG）混合壳层功能化的金纳米颗粒（NPs），为溶液中和表面上蛋白质的生物分子识别提供了一个有效的平台。具有明确结构的生物素化糖聚合物首先通过可逆加成-断裂链转移（RAFT）过程合成。它们含有两种类型的碳水化合物残基，即作为侧基的N-乙酰基-β-D-氨基葡萄糖吡喃糖苷（GlcNAc）或α-D-甘露糖吡喃糖苷（Man）。随后，生物素化糖聚合物和聚乙二醇通过简单的光化学过程用于原位形成金糖纳米颗粒。通过动态光散射（DLS）和透射电子显微镜（TEM）对所得的生物素化糖纳米颗粒进行了表征。使用衍射光学技术（DOT）系统评估了NPs外围生物素和特定碳水化合物残基的生物可利用性。研究表明，生物素配体可与DOTLab生物传感器上固定的抗生物素蛋白结合。此外，发现这些抗生物素蛋白偶联的糖纳米颗粒能选择性地固定凝集素。凝集素结合的特异性取决于碳水化合物残基的类型。因此，发现用N-乙酰基-β-D-氨基葡萄糖苷修饰的金纳米颗粒与麦胚凝集素（WGA）特异性相互作用，而用α-D-甘露糖苷修饰的金纳米颗粒与伴刀豆球蛋白A（Con A）特异性相互作用。
