2.50
Hdl Handle:
http://hdl.handle.net/2436/14648
Title:
Biological applications of the receptor mimetic peptide mastoparan.
Authors:
Jones, Sarah; Howl, John D.
Abstract:
The receptor mimetic and mast cell degranulating peptide mastoparan (MP) translocates cell membranes as an amphipathic alpha-helix, a feature that is undoubtedly a major determinant of bioactivity through the activation of heterotrimeric G proteins. Chimeric combinations of MP with G protein-coupled receptor (GPCR) ligands has produced peptides that exhibit biological activities distinct from their composite components. Thus, chimeric peptides such as galparan and M391 differentially modulate GTPase activity, display altered binding affinities for appropriate GPCRs and possess disparate secretory properties. MP and MP-containing chimerae also bind and modulate the activities of various other intracellular protein targets and are valuable tools to manipulate and study enzymatic activity, calcium homeostasis and apoptotic signalling pathways. In addition, charge delocalisation within the hydrophilic face of MP has produced analogues, including [Lys5, Lys8,Aib10]MP, that differentially regulate mast cell secretion and/or cytotoxicity. Finally, the identification of cell penetrant variants of MP chimerae has enabled the effective intracellular delivery of non-permeable biomolecules and presents an opportunity to target novel intracellular therapeutic loci.
Citation:
Current Protein & Peptide Science, 7(6): 501-508
Publisher:
Betham Science Publishers
Issue Date:
2006
URI:
http://hdl.handle.net/2436/14648
PubMed ID:
17168783
Additional Links:
http://www.bentham.org; http://www.ingentaconnect.com/content/ben/cpps/2006/00000007/00000006
Type:
Article
Language:
en
Description:
Metadata only
ISSN:
1389-2037
Appears in Collections:
Molecular Pharmacology Research Group

Full metadata record

DC FieldValue Language
dc.contributor.authorJones, Sarah-
dc.contributor.authorHowl, John D.-
dc.date.accessioned2007-11-19T12:35:55Z-
dc.date.available2007-11-19T12:35:55Z-
dc.date.issued2006-
dc.identifier.citationCurrent Protein & Peptide Science, 7(6): 501-508en
dc.identifier.issn1389-2037-
dc.identifier.pmid17168783-
dc.identifier.urihttp://hdl.handle.net/2436/14648-
dc.descriptionMetadata onlyen
dc.description.abstractThe receptor mimetic and mast cell degranulating peptide mastoparan (MP) translocates cell membranes as an amphipathic alpha-helix, a feature that is undoubtedly a major determinant of bioactivity through the activation of heterotrimeric G proteins. Chimeric combinations of MP with G protein-coupled receptor (GPCR) ligands has produced peptides that exhibit biological activities distinct from their composite components. Thus, chimeric peptides such as galparan and M391 differentially modulate GTPase activity, display altered binding affinities for appropriate GPCRs and possess disparate secretory properties. MP and MP-containing chimerae also bind and modulate the activities of various other intracellular protein targets and are valuable tools to manipulate and study enzymatic activity, calcium homeostasis and apoptotic signalling pathways. In addition, charge delocalisation within the hydrophilic face of MP has produced analogues, including [Lys5, Lys8,Aib10]MP, that differentially regulate mast cell secretion and/or cytotoxicity. Finally, the identification of cell penetrant variants of MP chimerae has enabled the effective intracellular delivery of non-permeable biomolecules and presents an opportunity to target novel intracellular therapeutic loci.en
dc.language.isoenen
dc.publisherBetham Science Publishersen
dc.relation.urlhttp://www.bentham.orgen
dc.relation.urlhttp://www.ingentaconnect.com/content/ben/cpps/2006/00000007/00000006en
dc.subjectPeptidesen
dc.subjectMast Cellsen
dc.subjectG protein-coupled receptorsen
dc.subjectCytotoxicityen
dc.subjectAminoisobutyric aciden
dc.subjectSignal Transductionen
dc.subjectMastoparan-
dc.titleBiological applications of the receptor mimetic peptide mastoparan.en
dc.typeArticleen
dc.format.digYES-

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