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

2.50
Hdl Handle:
http://hdl.handle.net/2436/29463
Title:
Interactions of cell penetrating peptide Tat with model membranes: a biophysical study.
Authors:
Dennison, Sarah R.; Baker, Rachael D.; Nicholl, Iain D.; Phoenix, David A.
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
Issue Date:
2007
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:
Article
Language:
en
ISSN:
0006-291X
Appears in Collections:
Cancer Research Group

Full metadata record

DC FieldValue Language
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): 178-182en
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.en
dc.language.isoenen
dc.publisherElsevier Science Directen
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)en
dc.subjectLipid monolayeren
dc.subjectIsothermen
dc.subjectTat peptideen
dc.subject.meshBinding Sitesen
dc.subject.meshBiomimeticsen
dc.subject.meshBiophysicsen
dc.subject.meshLipid Bilayersen
dc.subject.meshMembrane Fluidityen
dc.subject.meshMembranes, Artificialen
dc.subject.meshPeptide Fragmentsen
dc.subject.meshPhospholipidsen
dc.subject.meshProtein Bindingen
dc.subject.meshtat Gene Products, Human Immunodeficiency Virusen
dc.titleInteractions of cell penetrating peptide Tat with model membranes: a biophysical study.en
dc.typeArticleen
dc.identifier.journalBiochemical and Biophysical Research Communicationsen

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