The conformation of cyclo(-D-Pro-Ala4-) as a model for cyclic pentapeptides of the DL4 type.
The conformation of the cyclic pentapeptide cyclo(-D-Pro-Ala(4)-) 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.
Heller
Markus
M
Department Chemie, Technische Universität München, Lichtenbergstrasse 4, 85747 Garching, Germany.
Sukopp
Martin
M
Tsomaia
Natia
N
John
Michael
M
Mierke
Dale F
DF
Reif
Bernd
B
Kessler
Horst
H
D000409:Alanine / Q000031:analogs & derivatives*; D000595:Amino Acid Sequence; D001665:Binding Sites; D003198:Computer Simulation; D006860:Hydrogen Bonding; D007553:Isotope Labeling; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D010456:Peptides, Cyclic / Q000737:chemistry*; D011392:Proline / Q000031:analogs & derivatives*; D011487:Protein Conformation; D012996:Solutions / Q000737:chemistry; D013997:Time Factors
D010456:Peptides, Cyclic; D012996:Solutions; D011392:Proline; D000409:Alanine