The use of fluoresceinphosphatidylethanolamine (FPE) as a real-time probe for peptide-membrane interactions

Jonathan Wall, C. A. Golding, M. Van Veen, P. O'sheat

Research output: Contribution to journalArticle

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Abstract

The characterization of fluorescelnphosphatidylethanolamlne (FPE) as a real-time Indicator of the electrostatic nature of a membrane surface is described. The conditions appropriate for the labelling of membranes and the implementation of FPE as a tool to monitor the interactions of various peptides with model membranes are outlined. It is shown that of the membrane-active peptides studied, Naja naja kaouthla cardiotoxin and pyrularia thionin bind to certain model membranes without insertion. Whereas the leader sequence of the nuclear encoded subunit IV of mammalian cytochrome c oxidase (E.C. 1.9.3.1), known as p-25, and melittin appear to bind and then partially insert into the membrane. It seems evident also that melittin does not adopt a fully transmembrane configuration. Melittin is known to promote membrane lysis and by employing a rapid-kinetic technique it is shown that the time-course of such lysis does not appear to correlate with peptide binding, but following binding a significant proportion of melittin must become inserted into the membrane before lysis appears to commence.

Original languageEnglish (US)
Pages (from-to)183-192
Number of pages10
JournalMolecular Membrane Biology
Volume12
Issue number2
DOIs
StatePublished - Jan 1 1995

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Melitten
Peptides
Membranes
Pyrularia
Thionins
Cardiotoxins
Elapidae
Electron Transport Complex IV
Static Electricity

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cell Biology

Cite this

The use of fluoresceinphosphatidylethanolamine (FPE) as a real-time probe for peptide-membrane interactions. / Wall, Jonathan; Golding, C. A.; Veen, M. Van; O'sheat, P.

In: Molecular Membrane Biology, Vol. 12, No. 2, 01.01.1995, p. 183-192.

Research output: Contribution to journalArticle

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