Nuclear magnetic resonance study and secondary structure determination of the antibiotic peptide, aibellin.
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, 3JNHC alpha H coupling constants and amide hydrogen-deuterium (H-D) exchange rates show that the peptide consisted of two alpha-helices and a bent structure around a Pro-14 residue.
Kumazawa
S
S
Yokohama Research Center, Mitsubishi Chemical Corporation, Japan.
Kanda
M
M
Aoyama
H
H
Utagawa
M
M
Ohtani
H
H
Chiga
I
I
Mikawa
T
T
Hayase
T
T
Hino
T
T
D000595:Amino Acid Sequence; D000900:Anti-Bacterial Agents / Q000737:chemistry*; D023181:Antimicrobial Cationic Peptides; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D010455:Peptides; D017433:Protein Structure, Secondary
D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; D010455:Peptides; C083352:aibellin