Chapter title |
Engineering cyclic Peptide toxins.
|
---|---|
Book title |
Protein Engineering for Therapeutics, Part B
|
Published in |
Methods in enzymology, January 2012
|
DOI | 10.1016/b978-0-12-396962-0.00003-3 |
Pubmed ID | |
Book ISBNs |
978-0-12-396962-0
|
Authors |
Clark RJ, Craik DJ, Richard J. Clark, David J. Craik |
Abstract |
Peptide-based toxins have attracted much attention in recent years for their exciting potential applications in drug design and development. This interest has arisen because toxins are highly potent and selectively target a range of physiologically important receptors. However, peptides suffer from a number of disadvantages, including poor in vivo stability and poor bioavailability. A number of naturally occurring cyclic peptides have been discovered in plants, animals, and bacteria that have exceptional stability and potentially ameliorate these disadvantages. The lessons learned from studies of the structures, stabilities, and biological activities of these cyclic peptides can be applied to the reengineering of toxins that are not naturally cyclic but are amenable to cyclization. In this chapter, we describe solid-phase chemical synthetic methods for the reengineering of peptide toxins to improve their suitability as therapeutic, diagnostic, or imaging agents. The focus is on small disulfide-rich peptides from the venoms of cone snails and scorpions, but the technology is potentially widely applicable to a number of other peptide-based toxins. |
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Mendeley readers
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Computer Science | 1 | 2% |
Other | 0 | 0% |
Unknown | 11 | 22% |