title: Designing hybrid foldamers: the effect on the peptide conformational bias of β- versus α- and γ-linear residues in alternation with (1R,2S)-2-aminocyclobutane-1-carboxylic acid.
abstract: Several oligomers constructed with (1R,2S)-2-aminocyclobutane-1-carboxylic acid and glycine, β-alanine, and γ-amino butyric acid (GABA), respectively, joined in alternation have been synthesized and studied by means of NMR and CD experiments as well as with computational calculations. Results account for the spacer length effect on folding and show that conformational preference for these hybrid peptides can be tuned from β-sheet-like folding for those containing a C(2) or C(4) linear segment to a helical folding for those with a C(3) spacer between cyclobutane residues. The introduction of cyclic spacers between these residues does not modify the extended ribbon-type structure previously manifested in poly(cis-cyclobutane) β-oligomers.
authors: Departament de Química, Universitat Autònoma de Barcelona, Bellaterra, Spain.
authors: Sergio
authors: S
authors: Celis
authors: Esther
authors: E
authors: Gorrea
authors: Pau
authors: P
authors: Nolis
authors: Ona
authors: O
authors: Illa
authors: Rosa M
authors: RM
authors: Ortuño
mesh_terms: D000598:Amino Acids, Cyclic / Q000138:chemical synthesis / Q000737:chemistry*; D008958:Models, Molecular; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry*; D017510:Protein Folding; D017433:Protein Structure, Secondary; D015091:beta-Alanine / Q000138:chemical synthesis / Q000737:chemistry*; D005680:gamma-Aminobutyric Acid / Q000138:chemical synthesis / Q000737:chemistry*
chemical_list: C541323:2-aminocyclobutane-1-carboxylic acid; D000598:Amino Acids, Cyclic; D010455:Peptides; D015091:beta-Alanine; D005680:gamma-Aminobutyric Acid