Abstract: | Aibellin is a 20-residue peptide antibiotic that has been isolated from the fungus Verticimonosporium ellipticum. Sequence-specific assignment of the 1H- and 13C-NMR signals of aibellin in a methanol solution was achieved by using the two-dimensional NMR technique. Furthermore, its secondary structure was characterized by circular dichroism (CD) and NOESY spectra. The observed NOEs, 3JNHCαH coupling constants and amide hydrogen–deuterium (H–D) exchange rates show that the peptide consisted of two α-helices and a bent structure around a Pro-14 residue. |