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Interactions of cell penetrating peptide Tat with model membranes: a biophysical study.
Dennison, Sarah R. Baker, Rachael D. Nicholl, Iain D. Phoenix, David A.
Dennison, Sarah R.
Baker, Rachael D.
Nicholl, Iain D.
Phoenix, David A.
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Affiliation
Epub Date
Issue Date
2007
Submitted date
Alternative
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
Research Unit
PubMed ID
17854767
PubMed Central ID
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Type
Journal article
Language
en
Description
Series/Report no.
ISSN
0006-291X