|Title: ||Interactions of cell penetrating peptide Tat with model membranes: a biophysical study.|
|Citation: ||Biochemical and Biophysical Research Communications, 363(1): 178-182|
|Publisher: ||Elsevier Science Direct|
|Journal: ||Biochemical and Biophysical Research Communications|
|Issue Date: ||2007 |
|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|
|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.|
|Keywords: ||Cell Penetrating Peptides (CPP)|
|MeSH: ||Binding Sites|
tat Gene Products, Human Immunodeficiency Virus
|Appears in Collections: ||Cancer Research Group|
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