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    National Tsing Hua University Institutional Repository > 生命科學院  > 生命科學系 > 期刊論文 >  A Novel Cell-Penetrating Peptide Derived from Human Eosinophil Cationic Protein


    Please use this identifier to cite or link to this item: http://nthur.lib.nthu.edu.tw/dspace/handle/987654321/81431


    Title: A Novel Cell-Penetrating Peptide Derived from Human Eosinophil Cationic Protein
    Authors: Shun-lung Fang;Tan-chi Fan;Hua-Wen Fu;Chien-Jung Chen;Chi-Shin Hwang;Ta-Jen Hung;Lih-Yuan Lin;Margaret Dah-Tsyr Chang
    教師: 傅化文
    Date: 2013
    Publisher: Public Library of Science
    Relation: PLoS One, Public Library of Science, Volume 8, Issue 3, MAR 2013, e57318
    Keywords: MAJOR BASIC-PROTEIN
    SURFACE GLYCOSAMINOGLYCANS
    TRYPTOPHAN FLUORESCENCE
    MEMBRANE
    DELIVERY
    BINDING
    BIOSYNTHESIS
    ANTENNAPEDIA
    ENDOCYTOSIS
    MOLECULES
    Abstract: Cell-penetrating peptides (CPPs) are short peptides which can carry various types of molecules into cells; however, although most CPPs rapidly penetrate cells in vitro, their in vivo tissue-targeting specificities are low. Herein, we describe cell-binding, internalization, and targeting characteristics of a newly identified 10-residue CPP, denoted ECP^32-41, derived from the core heparin-binding motif of human eosinophil cationic protein (ECP). Besides traditional emphasis on positively charged residues, the presence of cysteine and tryptophan residues was demonstrated to be essential for internalization. ECP^32-41 entered Beas-2B and wild-type CHO-K1 cells, but not CHO cells lacking of cell-surface glycosaminoglycans (GAGs), indicating that binding of ECP^32-41 to cell-surface GAGs was required for internalization. When cells were cultured with GAGs or pre-treated with GAG-digesting enzymes, significant decreases in ECP^32-41 internalization were observed, suggesting that cell-surface GAGs, especially heparan sulfate proteoglycans were necessary for ECP^32-41 attachment and penetration. Furthermore, treatment with pharmacological agents identified two forms of energy-dependent endocytosis, lipid-raft endocytosis and macropinocytosis, as the major ECP^32-41 internalization routes. ECP^32-41 was demonstrated to transport various cargoes including fluorescent chemical, fluorescent protein, and peptidomimetic drug into cultured Beas-2B cells in vitro, and targeted broncho-epithelial and intestinal villi tissues in vivo. Hence this CPP has the potential to serve as a novel vehicle for intracellular delivery of biomolecules or medicines, especially for the treatment of pulmonary or gastrointestinal diseases.
    Relation Link: http://www.plos.org/
    URI: http://nthur.lib.nthu.edu.tw/dspace/handle/987654321/81431
    Appears in Collections:[分子與細胞生物研究所] 期刊論文
    [生命科學系] 期刊論文

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