Synthesis and peptide binding properties of methoxypyrrole amino acids (MOPAS).
[structure: see text] Methoxypyrrole amino acids (MOPAS) have been prepared and were introduced into small peptides with hairpin structures. The intra- and intermolecular binding properties of this heterocyclic amino acid mimicking a dipeptido beta-strand was investigated by NMR titration and X-ray crystal structure analysis. The data reveal a hydrogen bonding pattern that is complementary to a peptide beta-sheet.
Bonauer
Christoph
C
Institut für Organische Chemie and Zentrale Analytik, Universität Regensburg, D-93040 Regensburg, Germany.
Zabel
Manfred
M
König
Burkhard
B
D000596:Amino Acids / Q000138:chemical synthesis*; D018360:Crystallography, X-Ray; D006860:Hydrogen Bonding; D009682:Magnetic Resonance Spectroscopy; D008968:Molecular Conformation; D009842:Oligopeptides / Q000138:chemical synthesis / Q000737:chemistry*; D011485:Protein Binding; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D011758:Pyrroles / Q000737:chemistry*; D013237:Stereoisomerism
D000596:Amino Acids; D009842:Oligopeptides; D011758:Pyrroles