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

Howl, John D.; Jones, Sarah

dc.contributor.author	Howl, John D.
dc.contributor.author	Jones, Sarah
dc.date.accessioned	2008-06-25T15:42:20Z
dc.date.available	2008-06-25T15:42:20Z
dc.date.issued	2007
dc.identifier.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.
dc.identifier.uri	http://hdl.handle.net/2436/30466
dc.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.
dc.description.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.
dc.language.iso	en
dc.publisher	Australian Peptide Association
dc.relation.url	http://www.peptideoz.org/proceedings.php
dc.subject	Peptides
dc.subject	Cell Penetrating Peptides (CPP)
dc.subject	CPP
dc.subject	Rhegnylogic CPP
dc.subject	Biomedical applications
dc.title	Identification and biological applications of rhegnylogically-organized cell penetrating peptides.
dc.type	Conference contribution
refterms.dateFOA	2018-08-20T13:11:06Z
html.description.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.