NDLI: 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.

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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.

Content Provider	Semantic Scholar
Author	Celis, Sergio Gorrea, Esther Nolis, Pau Illa, Ona Ortuño, Rosa M.
Copyright Year	2012
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.
File Format	PDF HTM / HTML
DOI	10.1039/c1ob06575k
PubMed reference number	22130901
Journal	Medline
Volume Number	10
Issue Number	4
Alternate Webpage(s)	http://www.rsc.org/suppdata/ob/c1/c1ob06575k/c1ob06575k.pdf
Alternate Webpage(s)	https://doi.org/10.1039/c1ob06575k
Journal	Organic & biomolecular chemistry
Language	English
Access Restriction	Open
Content Type	Text
Resource Type	Article

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