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    Intracellular Target-Specific Accretion of Cell Penetrating Peptides and Bioportides: Ultrastructural and Biological Correlates

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    Authors
    Jones, Sarah
    Uusna, Julia
    Langel, Ülo
    Howl, John
    Issue Date
    2015-12-14
    
    Metadata
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    Abstract
    Cell penetrating peptide (CPP) technologies provide a viable strategy to regulate the activities of intracellular proteins that may be intractable to other biological agents. In particular, the cationic helical domains of proteins have proven to be a reliable source of proteomimetic bioportides, CPPs that modulate the activities of intracellular proteins. In this study we have employed live cell imaging confocal microscopy to determine the precise intracellular distribution of a chemically diverse set of CPPs and bioportides. Our findings indicate that, following efficient cellular entry, peptides are usually accreted at intracellular sites rather than being freely maintained in an aqueous cytosolic environment. The binding of CPPs to proteins in a relatively stable manner provides a molecular explanation for our findings. By extension, it is probable that many bioportides influence biological processes through a dominant-negative influence upon discrete protein–protein interactions. As an example, we report that bioportides derived from the leucine-rich repeat kinase 2 discretely influence the biology and stability of this key therapeutic target in Parkinson’s disease. The intracellular site-specific accretion of CPPs and bioportides can also be readily modulated by the attachment of larger cargoes or, more conveniently, short homing motifs. We conclude that site-specific intracellular targeting could be further exploited to expand the scope of CPP technologies.
    Citation
    Intracellular Target-Specific Accretion of Cell Penetrating Peptides and Bioportides: Ultrastructural and Biological Correlates
    Publisher
    American Chemical Society
    Journal
    Bioconjugate Chemistry
    URI
    http://hdl.handle.net/2436/621132
    DOI
    10.1021/acs.bioconjchem.5b00529
    Additional Links
    http://pubs.acs.org/doi/10.1021/acs.bioconjchem.5b00529
    Type
    Journal article
    Language
    en
    ISSN
    1043-1802
    1520-4812
    ae974a485f413a2113503eed53cd6c53
    10.1021/acs.bioconjchem.5b00529
    Scopus Count
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    Faculty of Science and Engineering

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