Screening of Paclitaxel-Binding Molecules from a Library of Random Peptides Displayed on T7 Phage Particles Using Paclitaxel-Photoimmobilized Resin

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• 作者：Sota Aoki ; Kengo Morohashi ; Takashi Sunoki ; Kouji Kuramochi ; Susumu Kobayashi ; Fumio Sugawara
• 刊名：Bioconjugate Chemistry
• 出版年：2007
• 出版时间：November 2007
• 年：2007
• 卷：18
• 期：6
• 页码：1981 - 1986
• 全文大小：767K
• 年卷期：v.18,no.6(November 2007)
• ISSN：1520-4812

文摘

Paclitaxel (Taxol), an effective anticancer agent, is known to bind to tubulin and induce tubulin polymerization. Several other binding proteins of paclitaxel, such as Bcl-2, heat shock proteins, and NSC-1, have also been reported. Here, we describe a T7 phage-based display to screen for paclitaxel-binding molecules from a random peptide library using paclitaxel-photoimmobilized TentaGel resin. Specific phage particles that bind the paclitaxel-immobilized resin were obtained. Among them, two phage clones included the same consensus amino acid sequence (KACGRTRVTS). Analysis of the protein database using BLAST revealed that a portion of this sequence is conserved in the zinc finger domain of human NFX1. Binding affinity of paclitaxel against the partial recombinant protein of NFX1 (424aa–876aa) was confirmed by pull-down assays and surface plasmon resonance analyses.