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Issue 3, 2018
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Side chain-specific 11/9-helix propensity of α/β-peptides with alternating residue types

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Abstract

The 11/9-helix is among the most stable and non-traditional helical structures for α/β-peptides with alternating residue types. The effect of side chain groups of α-residues and β3-residues on the 11/9-helix propensity was examined under various solvent conditions. An α-amino acid residue with one of the four representative side chain groups was incorporated into the central position of an α/β-pentapeptide backbone. A β-branched valine residue did not show any destabilizing effect. α,α-Dimethylsubstituted Aib residue was tolerated under nonpolar conditions, but did not promote 11/9-helical folding. The oligomer with a glycine residue did not show 11/9-helical folding under polar solvent conditions. The single unmatched stereochemistry of D-alanine was deleterious to 11/9-helical folding. Replacement of a cyclic β-residue with an acyclic β3-residue in the 11/9-helical structure had a slight destabilizing effect, which could be compensated by a longer peptide sequence with more cyclic β-residues. These results provide a guidance for incorporating functional groups into an 11/9-helical α/β-peptide backbone to design functional oligomers.

Graphical abstract: Side chain-specific 11/9-helix propensity of α/β-peptides with alternating residue types

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Publication details

The article was received on 16 Nov 2017, accepted on 07 Dec 2017 and first published on 07 Dec 2017


Article type: Paper
DOI: 10.1039/C7OB02816D
Citation: Org. Biomol. Chem., 2018,16, 433-438
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    Side chain-specific 11/9-helix propensity of α/β-peptides with alternating residue types

    J. Lee, J. Shim, P. Kang, M. Choi and S. H. Choi, Org. Biomol. Chem., 2018, 16, 433
    DOI: 10.1039/C7OB02816D

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