Biological identification of peptides that specifically bind to poly(phenylene vinylene) surfaces: Recognition of the branched or linear structure of the conjugated polymer

Hirotaka Ejima, Hisao Matsuno, Takeshi Serizawa

    研究成果: Contribution to journalArticle査読

    30 被引用数 (Scopus)

    抄録

    Peptides that bind to poly(phenylene vinylene) (PPV) were identified by the phage display method. Aromatic amino acids were enriched in these peptide sequences, suggesting that a π-π interaction is the key interaction between the peptides and PPV. The surface plasmon resonance (SPR) experiments using chemically synthesized peptides demonstrated that the Hyp01 peptide, with the sequence His-Thr-Asp-Trp-Arg-Leu-Gly-Thr-Trp-His-His-Ser, showed an affinity constant (7.7 × 105 M-1) for the target, hyperbranched PPV (hypPPV) film. This value is 15-fold greater than its affinity for linear PPV (lin PPV). In contrast, the peptide screened for lin PPV (Lin01) showed the reverse specificity for lin PPV. These results suggested that the Hyp01 and Lin01 peptides selectively recognized the linear or branched structure of PPVs. The Ala-scanning experiment, circular dichroism (CD) spectrometry, and molecular modeling of the Hyp01 peptide indicated that adequate location of two Trp residues by forming the polyproline type II (PII) helical conformation allowed the peptide to specifically interact with hypPPV.

    本文言語英語
    ページ(範囲)17278-17285
    ページ数8
    ジャーナルLangmuir
    26
    22
    DOI
    出版ステータス出版済み - 11 16 2010

    All Science Journal Classification (ASJC) codes

    • 材料科学(全般)
    • 凝縮系物理学
    • 表面および界面
    • 分光学
    • 電気化学

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