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

    Research output: Contribution to journalArticlepeer-review

    30 Citations (Scopus)

    Abstract

    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.

    Original languageEnglish
    Pages (from-to)17278-17285
    Number of pages8
    JournalLangmuir
    Volume26
    Issue number22
    DOIs
    Publication statusPublished - Nov 16 2010

    All Science Journal Classification (ASJC) codes

    • Materials Science(all)
    • Condensed Matter Physics
    • Surfaces and Interfaces
    • Spectroscopy
    • Electrochemistry

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