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    Interactions of cell penetrating peptide Tat with model membranes: a biophysical study.

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    Authors
    Dennison, Sarah R.
    Baker, Rachael D.
    Nicholl, Iain D.
    Phoenix, David A.
    Issue Date
    2007
    
    Metadata
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    Abstract
    The protein transduction domain of the HIV-1 transactivator of transcription, Tat (Tat((48-60))), has been shown to transport P10, a cytotoxic peptide mimic of the cyclin dependent kinase inhibitor p21WAF1/CIP1, into the nucleus of cancerous cells and induce apoptosis. Here, monolayer studies were used to investigate the membrane interactions of Tat((48-60)), P10 and the construct Tat((48-60))P10. It was found that Tat((48-60)) showed no significant surface activity but that both P10 and Tat((48-60))P10, were highly surface active, inducing surface pressure changes of 9.7 and 8.9mNm(-1), respectively, with DMPS monolayers. The comparison of Tat((48-60))P10 and P10 surface interactions would be consistent with a hypothesis that the cargo attachment influences the capacity of the Tat-protein transduction domain to mediate transport across membranes either directly or via localisation of the construct at the membrane interface.
    Citation
    Biochemical and Biophysical Research Communications, 363(1): 178-182
    Publisher
    Elsevier Science Direct
    Journal
    Biochemical and Biophysical Research Communications
    URI
    http://hdl.handle.net/2436/29463
    DOI
    10.1016/j.bbrc.2007.08.162
    PubMed ID
    17854767
    Additional Links
    http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6WBK-4PK8K5N-7&_user=10&_rdoc=1&_fmt=&_orig=search&_sort=d&view=c&_acct=C000050221&_version=1&_urlVersion=0&_userid=10&md5=79df9af6f737d67fceb156556b328c01
    Type
    Journal article
    Language
    en
    ISSN
    0006-291X
    ae974a485f413a2113503eed53cd6c53
    10.1016/j.bbrc.2007.08.162
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    Research Institute in Healthcare Science

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