Sculpting the beta-peptide foldamer H12 helix via a designed side-chain shape.
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.
Hetényi
Anasztázia
A
Institute of Pharmaceutical Chemistry, University of Szeged, H-6720, Szeged, Hungary.
Szakonyi
Zsolt
Z
Mándity
István M
IM
Szolnoki
Eva
E
Tóth
Gábor K
GK
Martinek
Tamás A
TA
Fülöp
Ferenc
F
D002264:Carboxylic Acids / Q000737:chemistry*; D003508:Cycloheptanes / Q000737:chemistry*; D004123:Dimethylamines / Q000737:chemistry*; D015394:Molecular Structure; D009842:Oligopeptides / Q000737:chemistry*; D017510:Protein Folding; D017433:Protein Structure, Secondary; D013237:Stereoisomerism
D002264:Carboxylic Acids; D003508:Cycloheptanes; D004123:Dimethylamines; D009842:Oligopeptides