Protein-Directed Immobilization of Phosphocholine Ligands on a Gold Surface for Multivalent C-Reactive Protein Binding

Author(s): Eunjoo Kim, Se Geun Lee, Hyun-Chul Kim, Sung Jun Lee, Chul Su Baek, Sang Won Jeong.

Journal Name: Current Topics in Medicinal Chemistry

Volume 13 , Issue 4 , 2013

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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.

Keywords: Synthetic receptor, multivalent protein binding, directed immobilization, C-reactive protein, phosphocholine, molecular imprinting, surface plasmon resonance.

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Article Details

Year: 2013
Page: [519 - 524]
Pages: 6
DOI: 10.2174/1568026611313040012
Price: $58

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