Spatial structure determination of antiarrhythmic peptide using nuclear magnetic resonance spectroscopy.
The peptide AAP10 was synthesized according to the Merrifield technique following the Fmoc-strategy and its spatial structure in aqueous solution studied with NMR principles. It is known from previous studies that the peptide has antiarrhythmic activity and inhibits cardiac ischemia induced alterations of the activation pattern, decreases the activation-recovery interval (ARI) dispersion and improves cellular coupling via enhancement of gap junction conductance (2, 2, 3, 4). The peptide was synthesized as a peptide amide. Two different semi cyclic conformations were characterized.
Grover
R
R
Institute of Pharmacology, University of Cologne, Germany.
Dhein
S
S
D000889:Anti-Arrhythmia Agents / Q000138:chemical synthesis / Q000737:chemistry*; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D009842:Oligopeptides / Q000138:chemical synthesis / Q000737:chemistry*; D011487:Protein Conformation
C090806:AAP 10; D000889:Anti-Arrhythmia Agents; D009842:Oligopeptides; C029579:antiarrhythmic peptide