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Protein-Directed Immobilization of Phosphocholine Ligands on a Gold Surface for Multivalent C-Reactive Protein Binding
- Protein-Directed Immobilization of Phosphocholine Ligands on a Gold Surface for Multivalent C-Reactive Protein Binding
- Kim, Eunjoo; Lee, Se Geun; Kim, Hyun-Chul; Lee, Sung Jun; Baek, Chul Su; Jeong, Sang Won
- DGIST Authors
- Kim, Eunjoo; Lee, Se Geun; Kim, Hyun-Chul; Lee, Sung Jun; Jeong, Sang Won
- Issue Date
- Current Topics in Medicinal Chemistry, 13(4), 519-524
- Article Type
- 12 Mercaptododecylphosphocholine; Binding Affinity; Binding Sites; C-Reactive Protein; C Reactive Protein; Column Chromatography; Controlled Study; Directed Immobilization; Gold; Human; Humans; Ligands; Mercaptoethanol; Molecular Imprinting; Monolayer Culture; Multivalent Protein Binding; Phosphocholine; Phosphorylcholine; Protein Binding; Protein Immobilization; Protein Synthesis; Surface Plasmon Resonance; Surface Properties; Synthetic Receptor; Unclassified Drug
- The preparation of a synthetic receptor for multivalent protein binding by a directed immobilization of bifunctional ligands was demonstrated using pentameric C-reactive protein (CRP) and a thiolated phosphocholine-containing ligand on a gold surface. CRP consisting of five identical, noncovalently linked subunits and having five phosphocholinebinding sites on the same face was complexed with 12-mercaptododecylphosphocholine. The complexes were reacted with a gold surface, which was blocked with BSA or 2-mercaptoethanol to avoid non-specific binding. CRP binding to the molecularly imprinted monolayer was investigated by surface plasmon resonance, exhibiting high sensitivity with a detection limit as low as 1 pM (0.12 ng/mL) and binding affinity (KA ∼ 10-7-10-9 M-1) comparable to that of immobilized anti-CRP. © 2013 Bentham Science Publishers.
- Bentham Science Publisher
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