Sculpting the beta-peptide foldamer H12 helix via a designed side-chain shape

Author
Abstract

The long-range side-chain repulsion between the (1R, 2R, 3R, 5R)-2- amino-6,6-dimethyl-bicyclo[3.1.1]-heptane-3-carboxylic acid (trans-ABHC) residues stabilize the H12 helix in beta-peptide oligomers.

Year of Publication
2009
Journal
Chemical Communications
Number of Pages
177–179
ISSN Number
1359-7345
URL
https://doi.org/10.1039/B812114A
DOI
10.1039/B812114A
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