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

TitleSculpting the beta-peptide foldamer H12 helix via a designed side-chain shape
Publication TypeJournal Article
Year of Publication2009
AuthorsHetenyi, A, Szakonyi, Z, Mándity, IM, Szolnoki, E, Toth, GK, Martinek, TA, Fülöp, F
JournalChemical Communications
Pagination177–179
ISSN1359-7345
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.