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Bulletin of the Korean Chemical Society (BKCS)

ISSN 0253-2964(Print)
ISSN 1229-5949(Online)
Volume 34, Number 9
BKCSDE 34(9)
September 20, 2013 

Comparison of Oct-2-enyl and Oct-4-enyl Staples for Their Formation and α-Helix Stabilizing Effects
Thanh K. Pham, Jiyeon Yoo, Young-Woo Kim*
α-Helix, Stapled peptides, Ring-closing metathesis, Protease resistance, Peptide drugs
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 α-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 α-helix induction. The data further increases the understanding of the structure-activity relationships of this valuable chemical tool.
2640 - 2644
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