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

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

Volume: 13 Issue: 4

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

Affiliation:

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

Abstract: 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 (K_A ~ 10^-7-10^-9 M^-1) comparable to that of immobilized anti- CRP.

Cite this article as:

Kim Eunjoo, Lee Se Geun, Kim Hyun-Chul, Lee Sung Jun, Baek Chul Su and Jeong Sang Won, Protein-Directed Immobilization of Phosphocholine Ligands on a Gold Surface for Multivalent C-Reactive Protein Binding, Current Topics in Medicinal Chemistry 2013; 13 (4) . https://dx.doi.org/10.2174/1568026611313040012