Identification of a methotrexate-binding peptide from a T7 phage display screen using a QCM device.

Yoichi Takakusagi, Yuki Kuroiwa, Fumio Sugawara, Kengo Sakaguchi

Department of Applied Biological Science, Faculty of Science and Technology, Tokyo University of Science, 2641 Yamazaki, Noda, Chiba 278-8510, Japan.

Bioorganic & medicinal chemistry 2008 Aug 1

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An 11-mer unique peptide sequence SIFPLCNSGAL was identified as a methotrexate (MTX)-binding peptide from a T7 phage display screen using a quartz-crystal microbalance (QCM) biosensor. The synthetic peptide displayed weak interaction with MTX (K(D) 2.23x10(-5) M) using surface plasmon resonance (SPR). Interestingly, analysis of the primary amino acid sequence of the peptide identified similarities to the MTX-binding site of dihydrofolate reductase (DHFR). Our results highlight the importance of this primary sequence for the recognition of the MTX molecule.

Citation

Yoichi Takakusagi, Yuki Kuroiwa, Fumio Sugawara, Kengo Sakaguchi. Identification of a methotrexate-binding peptide from a T7 phage display screen using a QCM device. Bioorganic & medicinal chemistry. 2008 Aug 1;16(15):7410-4