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Merck

High-performance affinity beads for identifying drug receptors.

Nature biotechnology (2000-08-10)
N Shimizu, K Sugimoto, J Tang, T Nishi, I Sato, M Hiramoto, S Aizawa, M Hatakeyama, R Ohba, H Hatori, T Yoshikawa, F Suzuki, A Oomori, H Tanaka, H Kawaguchi, H Watanabe, H Handa
RESUMEN

We have developed a method using novel latex beads for rapid identification of drug receptors using affinity purification. Composed of a glycidylmethacrylate (GMA) and styrene copolymer core with a GMA polymer surface, the beads minimize nonspecific protein binding and maximize purification efficiency. We demonstrated their performance by efficiently purifying FK506-binding protein using FK506-conjugated beads, and found that the amount of material needed was significantly reduced compared with previous methods. Using the latex beads, we identified a redox-related factor, Ref-1, as a target protein of an anti-NF-kappaB drug, E3330, demonstrating the existence of a new class of receptors of anti-NF-kappaB drugs. Our results suggest that the latex beads could provide a tool for the identification and analysis of drug receptors and should therefore be useful in drug development.

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Sigma-Aldrich
E3330, ≥98% (HPLC)