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Side chain-specific 11/9-helix propensity of α/β-peptides with alternating residue types.
| Content Provider | Semantic Scholar |
|---|---|
| Author | Lee, Jaeyeon Shim, Jihyun Kang, Philjae Choi, Moon-Gun Choi, Soo Hyuk |
| Copyright Year | 2018 |
| 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. |
| Starting Page | 433 |
| Ending Page | 438 |
| Page Count | 6 |
| File Format | PDF HTM / HTML |
| DOI | 10.1039/c7ob02816d |
| Alternate Webpage(s) | http://www.rsc.org/suppdata/c7/ob/c7ob02816d/c7ob02816d1.pdf |
| PubMed reference number | 29264605 |
| Alternate Webpage(s) | https://doi.org/10.1039/c7ob02816d |
| Journal | Medline |
| Volume Number | 16 |
| Issue Number | 3 |
| Journal | Organic & biomolecular chemistry |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |
