Show simple item record

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

dc.contributor.authorDennison, Sarah R.
dc.contributor.authorBaker, Rachael D.
dc.contributor.authorNicholl, Iain D.
dc.contributor.authorPhoenix, David A.
dc.date.accessioned2008-06-04T10:45:06Z
dc.date.available2008-06-04T10:45:06Z
dc.date.issued2007
dc.identifier.citationBiochemical and Biophysical Research Communications, 363(1): 178-182
dc.identifier.issn0006-291X
dc.identifier.pmid17854767
dc.identifier.doi10.1016/j.bbrc.2007.08.162
dc.identifier.urihttp://hdl.handle.net/2436/29463
dc.description.abstractThe 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.
dc.language.isoen
dc.publisherElsevier Science Direct
dc.relation.urlhttp://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
dc.subjectCell Penetrating Peptides (CPP)
dc.subjectLipid monolayer
dc.subjectIsotherm
dc.subjectTat peptide
dc.subject.meshBinding Sites
dc.subject.meshBiomimetics
dc.subject.meshBiophysics
dc.subject.meshLipid Bilayers
dc.subject.meshMembrane Fluidity
dc.subject.meshMembranes, Artificial
dc.subject.meshPeptide Fragments
dc.subject.meshPhospholipids
dc.subject.meshProtein Binding
dc.subject.meshtat Gene Products, Human Immunodeficiency Virus
dc.titleInteractions of cell penetrating peptide Tat with model membranes: a biophysical study.
dc.typeJournal article
dc.identifier.journalBiochemical and Biophysical Research Communications
html.description.abstractThe 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.


Files in this item

Thumbnail
Name:
Publisher version

This item appears in the following Collection(s)

Show simple item record