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The Conformation of cyclo(−d-Pro−Ala4−) as a Model for Cyclic Pentapeptides of the dL4 Type
journal contribution
posted on 2006-10-25, 00:00 authored by Markus Heller, Martin Sukopp, Natia Tsomaia, Michael John, Dale F. Mierke, Bernd Reif, Horst KesslerThe conformation of the cyclic pentapeptide cyclo(−d-Pro−Ala4−) 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.