Grauer, Andreas and Cabrele, C. and Zabel, M. and König, Burkhard (2009) Stable right- and left-handed peptide helices containing Cα-tetrasubstituted α amino acids. The Journal of Organic Chemistry 74 (10), pp. 3718-3726.
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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 Cα-tetrasubstituted α-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 right-handed 310-helices, while the all-R-configured peptides 11−13 (RR)2−4 form left-handed 310-helices in the solid state and solution.
|Institutions:|| Chemistry and Pharmacy > Institut für Organische Chemie > Lehrstuhl Prof. Dr. Burkhard König|
Chemistry and Pharmacy > Institut für Anorganische Chemie > Arbeitskreis Prof. Dr. Nikolas Korber
|Projects:||GRK 760, Graduiertenkolleg Medizinische Chemie|
|Subjects:||500 Science > 540 Chemistry & allied sciences|
|Created at the University of Regensburg:||Yes|
|Deposited On:||23 Jun 2009 17:45|
|Last Modified:||26 Oct 2010 11:22|
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