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

[ Vol. 13 , Issue. 4 ]


Eunjoo Kim, Se Geun Lee, Hyun-Chul Kim, Sung Jun Lee, Chul Su Baek and Sang Won Jeong   Pages 519 - 524 ( 6 )


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.


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


Nano & Bio Research Division, Daegu Gyeongbuk Institute of Science and Technology (DGIST), Daegu 711-873, Korea.

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