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http://dx.doi.org/10.5012/bkcs.2013.34.9.2640

Comparison of Oct-2-enyl and Oct-4-enyl Staples for Their Formation and α-Helix Stabilizing Effects  

Pham, Thanh K. (College of Pharmacy, Dongguk University)
Yoo, Jiyeon (College of Pharmacy, Dongguk University)
Kim, Young-Woo (College of Pharmacy, Dongguk University)
Publication Information
Bulletin of the Korean Chemical Society / v.34, no.9, 2013 , pp. 2640-2644 More about this Journal
Abstract
The all-hydrocarbon i,i+4 stapling system using an oct-4-enyl crosslink is one of the most widely employed chemical tools to stabilize an ${\alpha}$-helical conformation of a short peptide. This crosslinking system has greatly extended our ability to modulate intracellular protein-macromolecule interactions. The helix-inducing property of the i,i+4 staple has shown to be highly dependent on the length and the stereochemistry of the oct-4-enyl crosslink. Here we show that changing the double bond position within the i,i+4 staple has a considerable impact not only on the formation of the crosslink but also on ${\alpha}$-helix induction. The data further increases the understanding of the structure-activity relationships of this valuable chemical tool.
Keywords
${\alpha}$-Helix; Stapled peptides; Ring-closing metathesis; Protease resistance; Peptide drugs;
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