Grauer, Andreas A. and Cabrele, Chiara and Zabel, Manfred and Koenig, Burkhard (2009) Stable Right- and Left-Handed Peptide Helices containing C-alpha-Tetrasubstituted alpha-Amino Acids. JOURNAL OF ORGANIC CHEMISTRY, 74 (10). pp. 3718-3726. ISSN 0022-3263,
Full text not available from this repository. (Request a copy)Abstract
Short peptidomimetics with stable secondary structures in solution are of interest for applications in chemistry, biology, and medicine. One way to rigidify the backbone of a peptide is the use of cyclic C-alpha-tetrasubstituted alpha-amino acids (TAAs) like compound 14. The structures resulting from the incorporation of this unnatural amino acid into peptides were investigated. In total, 13 different peptides with a length of up to eight residues and alternating sequences of TAA 14 and (S)- or (R)-valine were synthesized. Their structures were characterized by X-ray diffraction analysis and NMR and CD measurements showing that the all-S-backbone-configured peptides 5 and 6 (SS)(2-3) form fight-handed 3(10)-helices, while the all-R-configured peptides 11-13 (RR)(2-4) form left-handed 3(10)-helices in the solid state and solution.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | MAGNETIC-RESONANCE SPECTROSCOPY; O BOND FORMATION; CONFORMATIONAL PREFERENCES; BIOACTIVE PEPTIDES; STEREOSELECTIVE-SYNTHESIS; 3-DIMENSIONAL STRUCTURES; ASYMMETRIC-SYNTHESIS; BETA-TURNS; PART 2; PROTEINS; |
| Subjects: | 500 Science > 540 Chemistry & allied sciences |
| Divisions: | Chemistry and Pharmacy > Institut für Organische Chemie > Lehrstuhl Prof. Dr. Burkhard König |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 15 Sep 2020 11:05 |
| Last Modified: | 15 Sep 2020 11:05 |
| URI: | https://pred.uni-regensburg.de/id/eprint/28976 |
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