The Conformation of <i>cyclo</i>(−d-Pro−Ala<sub>4</sub>−) as a Model for
Cyclic Pentapeptides of the dL<sub>4</sub> Type
Markus Heller
Martin Sukopp
Natia Tsomaia
Michael John
Dale F. Mierke
Bernd Reif
Horst Kessler
10.1021/ja063174a.s001
https://acs.figshare.com/articles/journal_contribution/The_Conformation_of_i_cyclo_i_d_Pro_Ala_sub_4_sub_as_a_Model_for_Cyclic_Pentapeptides_of_the_dL_sub_4_sub_Type/3051937
The conformation of the cyclic pentapeptide <i>cyclo</i>(−d-Pro−Ala<sub>4</sub>−) in solution and in the solid
state was reinvestigated using modern NMR techniques. To allow unequivocal characterization of hydrogen
bonds, relaxation behavior, and intramolecular distances, differently labeled isotopomers were synthesized.
The NMR results, supported by extensive MD simulations, demonstrate unambiguously that the preferred
conformation previously described by us, but recently questioned, is indeed correct. The validation of the
conformational preferences of this cyclic peptide is important given that this system is a template for several
bioactive compounds and for controlled “spatial screening” for the search of bioactive conformations.
2006-10-25 00:00:00
dL 4 TypeThe conformation
Cyclic Pentapeptides
intramolecular distances
bioactive compounds
NMR results
hydrogen bonds
relaxation behavior
cyclo
bioactive conformations
MD simulations
cyclic peptide
NMR techniques