Identification and biological applications of rhegnylogically-organized cell penetrating peptides.

2.50
Hdl Handle:
http://hdl.handle.net/2436/30466
Title:
Identification and biological applications of rhegnylogically-organized cell penetrating peptides.
Authors:
Howl, John D.; Jones, Sarah
Abstract:
Introduction: Many different cell penetrating peptides (CPPs) have been utilized as vectors to affect the highly efficient intracellular delivery of bioactive moieties. A majority of such studies employ sychnologically-organized tandem combinations of a cargo (message) and a CPP (address). To date, bioactive cargoes have included peptides, proteins and a range of oligonucleotides attached either by direct chemical conjugation or as a component of a larger macromolecular complex. Moreover, a majority of CPPs, including the commonly used sequences Tat and penetratin, are designed to be both biologically and toxicologically inert. More recently, a QSAR-based algorithm has been developed to predict cryptic polycationic CPP motifs within the primary sequences of proteins. As described here, this novel technology has enabled the study of rhegnylogic CPPs in which multiple pharmacophores for cellular penetration and desirable biological activities are discontinuously organized within the primary sequence of single peptide. This organization differs from the more commonly utilized sychnologic strategy which joins functionally discrete and continous address and messages together in a tandem construct.
Citation:
In: Wilce, J. (Ed.), Proceedings of the 4th International Peptide Symposium, in conjunction with the 7th Australian Peptide Conference and the 2nd Asia-Pacific International Peptide Symposium, 21-25 October 2007, Cairns, Great Barrier Reef, Queensland, Australia.
Publisher:
Australian Peptide Association
Issue Date:
2007
URI:
http://hdl.handle.net/2436/30466
Additional Links:
http://www.peptideoz.org/proceedings.php
Type:
Meetings & Proceedings
Language:
en
Description:
Acknowledgments: We are extremely grateful to Ülo Langel (Stockholm) who provided access to the CPP prediction algorithm. This work also benefited from collaborations with Shant Kumar (Manchester) and Matjaž Zorko (Ljubljana). These investigations were financially supported in part by the Samantha Dickson Brain Tumour Trust.
Appears in Collections:
Molecular Pharmacology Research Group

Full metadata record

DC FieldValue Language
dc.contributor.authorHowl, John D.-
dc.contributor.authorJones, Sarah-
dc.date.accessioned2008-06-25T15:42:20Z-
dc.date.available2008-06-25T15:42:20Z-
dc.date.issued2007-
dc.identifier.citationIn: Wilce, J. (Ed.), Proceedings of the 4th International Peptide Symposium, in conjunction with the 7th Australian Peptide Conference and the 2nd Asia-Pacific International Peptide Symposium, 21-25 October 2007, Cairns, Great Barrier Reef, Queensland, Australia.en
dc.identifier.urihttp://hdl.handle.net/2436/30466-
dc.descriptionAcknowledgments: We are extremely grateful to Ülo Langel (Stockholm) who provided access to the CPP prediction algorithm. This work also benefited from collaborations with Shant Kumar (Manchester) and Matjaž Zorko (Ljubljana). These investigations were financially supported in part by the Samantha Dickson Brain Tumour Trust.en
dc.description.abstractIntroduction: Many different cell penetrating peptides (CPPs) have been utilized as vectors to affect the highly efficient intracellular delivery of bioactive moieties. A majority of such studies employ sychnologically-organized tandem combinations of a cargo (message) and a CPP (address). To date, bioactive cargoes have included peptides, proteins and a range of oligonucleotides attached either by direct chemical conjugation or as a component of a larger macromolecular complex. Moreover, a majority of CPPs, including the commonly used sequences Tat and penetratin, are designed to be both biologically and toxicologically inert. More recently, a QSAR-based algorithm has been developed to predict cryptic polycationic CPP motifs within the primary sequences of proteins. As described here, this novel technology has enabled the study of rhegnylogic CPPs in which multiple pharmacophores for cellular penetration and desirable biological activities are discontinuously organized within the primary sequence of single peptide. This organization differs from the more commonly utilized sychnologic strategy which joins functionally discrete and continous address and messages together in a tandem construct.en
dc.language.isoenen
dc.publisherAustralian Peptide Associationen
dc.relation.urlhttp://www.peptideoz.org/proceedings.phpen
dc.subjectPeptidesen
dc.subjectCell Penetrating Peptides (CPP)en
dc.subjectCPPen
dc.subjectRhegnylogic CPPen
dc.subjectBiomedical applicationsen
dc.titleIdentification and biological applications of rhegnylogically-organized cell penetrating peptides.en
dc.typeMeetings & Proceedingsen
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