2.50
Hdl Handle:
http://hdl.handle.net/2436/29937
Title:
Chimerism: a strategy to expand the utility and applications of peptides
Authors:
Howl, John D.
Other Titles:
Peptide Synthesis and Applications: 25-41
Abstract:
The modular nature of peptides can be exploited in the synthesis of chimeric sequences that combine diverse motifs in a single molecule. A theoretical consideration of the classification of peptides further expounds the multigeneric nature of peptide chimeras. Strategies for chimeric peptide syntheses include the chemical cross-linking of monomers and tandem combination by conventional SPPS. Additional details of chimeric peptide synthesis are also provided elsewhere in this volume. This chapter also explores some of the more common applications of chimeric peptides with particular emphasis on the molecular pharmacology of sequences that include address motifs for G protein-coupled receptors. Specific details of the biological properties of chimeras containing mastoparan, an amphiphilic tetradecapeptide component of wasp venom, further illustrate the novel and often unpredictable biological actions of chimeric constructs. These and numerous additional studies confirm that chimerism is an established strategy for the synthesis of molecular probes and bioactive agents.
Citation:
Methods in Molecular Biology, 298: 25-41
Publisher:
Clifton, N.J.: Humana Press
Journal:
Methods in Molecular Biology
Issue Date:
2005
URI:
http://hdl.handle.net/2436/29937
DOI:
10.1385/1592598773
PubMed ID:
16044538
Additional Links:
http://www.springerlink.com/content/r1541637h477n439/
Type:
Article; Book chapter
Language:
en
Description:
This article is published as a chapter in a book but is also cited as an article in a journal series
ISSN:
1064-3745
ISBN:
978-1588293176; 978-1592598779
Appears in Collections:
Molecular Pharmacology Research Group

Full metadata record

DC FieldValue Language
dc.contributor.authorHowl, John D.-
dc.date.accessioned2008-06-12T08:33:14Z-
dc.date.available2008-06-12T08:33:14Z-
dc.date.issued2005-
dc.identifier.citationMethods in Molecular Biology, 298: 25-41en
dc.identifier.isbn978-1588293176-
dc.identifier.isbn978-1592598779-
dc.identifier.issn1064-3745-
dc.identifier.pmid16044538-
dc.identifier.doi10.1385/1592598773-
dc.identifier.urihttp://hdl.handle.net/2436/29937-
dc.descriptionThis article is published as a chapter in a book but is also cited as an article in a journal seriesen
dc.description.abstractThe modular nature of peptides can be exploited in the synthesis of chimeric sequences that combine diverse motifs in a single molecule. A theoretical consideration of the classification of peptides further expounds the multigeneric nature of peptide chimeras. Strategies for chimeric peptide syntheses include the chemical cross-linking of monomers and tandem combination by conventional SPPS. Additional details of chimeric peptide synthesis are also provided elsewhere in this volume. This chapter also explores some of the more common applications of chimeric peptides with particular emphasis on the molecular pharmacology of sequences that include address motifs for G protein-coupled receptors. Specific details of the biological properties of chimeras containing mastoparan, an amphiphilic tetradecapeptide component of wasp venom, further illustrate the novel and often unpredictable biological actions of chimeric constructs. These and numerous additional studies confirm that chimerism is an established strategy for the synthesis of molecular probes and bioactive agents.en
dc.language.isoenen
dc.publisherClifton, N.J.: Humana Pressen
dc.relation.urlhttp://www.springerlink.com/content/r1541637h477n439/en
dc.subjectChimerismen
dc.subjectGalparanen
dc.subjectVasopressinen
dc.subjectG protein-coupled receptorsen
dc.subjectLigand bindingen
dc.subjectMastoparanen
dc.subjectsecretionen
dc.subjectGenomicsen
dc.subjectPeptide Mastoparanen
dc.subject.meshAmino Acid Sequenceen
dc.subject.meshAnimalsen
dc.subject.meshCell Lineen
dc.subject.meshHumansen
dc.subject.meshLigandsen
dc.subject.meshMolecular Biologyen
dc.subject.meshMolecular Sequence Dataen
dc.subject.meshPeptidesen
dc.subject.meshRatsen
dc.subject.meshReceptors, G-Protein-Coupleden
dc.subject.meshReceptors, Vasopressinen
dc.subject.meshRecombinant Fusion Proteinsen
dc.subject.meshWasp Venomsen
dc.subject.meshbeta-N-Acetylhexosaminidasesen
dc.titleChimerism: a strategy to expand the utility and applications of peptidesen
dc.title.alternativePeptide Synthesis and Applications: 25-41en
dc.typeArticleen
dc.typeBook chapteren
dc.identifier.journalMethods in Molecular Biologyen

Related articles on PubMed

All Items in WIRE are protected by copyright, with all rights reserved, unless otherwise indicated.