title: Self-association-driven transition of the β-peptidic H12 helix to the H18 helix.
abstract: Various patterns of foldameric oligomers formed by trans-ABHC ((1S,2S,3S,5S)-2-amino-6,6-dimethylbicyclo[3.3.1]heptane-3-carboxylic acid) and β(3)-hSer residues were studied. NMR, ECD and molecular modelling demonstrated that octameric and nonameric sequences with multiple i-i+3 ABHC pair repulsions attain the β-H18 helix in CD(3)OH. As a close relative of the α-helix, this helix type is stabilized by i-i+4 backbone H-bond interactions. The formation of the β-H18 helix was found to be solvent- and concentration-dependent. Upon dilution, the β-H18 → β-H12 helix transition was revealed by concentration-dependent ECD, DOSY-NMR and TEM measurements.
authors: Institute of Pharmaceutical Chemistry, University of Szeged, Eötvös u. 6., H-6720 Szeged, Hungary.
authors: Eva
authors: E
authors: Szolnoki
authors: Anasztázia
authors: A
authors: Hetényi
authors: Tamás A
authors: TA
authors: Martinek
authors: Zsolt
authors: Z
authors: Szakonyi
authors: Ferenc
authors: F
authors: Fülöp
mesh_terms: D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry*; D017433:Protein Structure, Secondary
chemical_list: D010455:Peptides