Solution structure of an antimicrobial peptide buforin II.
The structure of 21-residue antimicrobial peptide buforin II has been determined by using NMR spectroscopy and restrained molecular dynamics. Buforin II adopts a flexible random structure in H2O. In trifluoroethanol (TFE)/H2O (1:1, v/v) mixture, however, buforin II assumes a regular alpha-helix between residues Val12 and Arg20 and a distorted helical structure between residues Gly7 and Pro11. The model structure obtained shows an amphipathic character in the region from Arg5 to the C-terminus, Lys21. Like other known cationic antimicrobial peptides, the amphipathic structure might be the key factor for antimicrobial activity of buforin II.
Yi
G S
GS
Magnetic Resonance Group, Korea Basic Science Institute, Taejon, South Korea.
Park
C B
CB
Kim
S C
SC
Cheong
C
C
D000595:Amino Acid Sequence; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry* / Q000494:pharmacology*
D011506:Proteins; C097849:buforin II